Cytisus

Hideyuki Yamasawa, President and Chief Executive Officer

Cytochrome bc1

Cytogenetics (journal)

Cytogenetics is a branch of genetics that is concerned with the study of the structure and function of the cell, especially the chromosomes. It includes routine analysis of G-banded chromosomes, other cytogenetic banding techniques, as well as molecular cytogenetics such as fluorescent in situ hybridization (FISH) and comparative genomic hybridization (CGH).

changed

The cytochrome complex, or cyt c is a small hemeprotein found loosely associated with the inner membrane of the mitochondrion. It belongs to the cytochrome c family of proteins. Cytochrome c is highly water-soluble, unlike other cytochromes, and is an essential component of the electron transport chain, where it carries one electron. It is capable of undergoing oxidation and reduction, but does not bind oxygen.

Cytisus ramentaceus

Cytir Mawr

Cytidine triphosphate

Cytochrome b is a protein found in the mitochondria of eukaryotic cells. It functions as part of the electron transport chain and is the main subunit of transmembrane cytochrome bc1 and b6f complexes.

Structure of the 13-subunit oxidized cytochrome c oxidase.

Cytochrome Oxidase Subunit 1

Virtuoso pianist, pedagogue

Sweet

Cytochrome d

Cytohematology

Space-filling model of the Cytidine diphosphate molecule as an anion

Cytofol

COX3

Cytidine diphosphate glucose.png

Cytochrome P-450 reductase

Cytochalasin D is a member of the class of mycotoxins known as cytochalasins. Cytochalasin D is an alkaloid produced by Helminthosporium and other molds.Cytochalasin D is a cell-permeable and potent inhibitor of actin polymerization. It disrupts actin microfilaments and activates the p53-dependent pathways causing arrest of the cell cycle at the G1-S transition. It is believed to bind to F-actin polymer and prevent polymerization of actin monomers.

Cytinus hypocistis is an ant-pollinated species of parasitic plant in the family Cytinaceae having four subspecies. It is found primarily in locations that surround the Mediterranean Sea, and is the type for the genus Cytinus. The binomial has been conserved.

In enzymology, a cytidylate cyclase (EC 4.6.1.6) is an enzyme that catalyzes the chemical reactionCTP ⇌ {\displaystyle \rightleftharpoons } 3',5'-cyclic CMP + diphosphateHence, this enzyme has one substrate, CTP, and two products, 3',5'-cyclic CMP and diphosphate.This enzyme belongs to the family of lyases, specifically the class of phosphorus-oxygen lyases.

Zygosporin A; Cytohalasin D; Lygosporin A

Cytochrome-c oxidase

Cytochrome P-450 CYP1A1

COX1 or COI

Cytochrome b559, alpha and beta subunits

Cytisus scoparius, the common broom or Scotch broom, syn. Sarothamnus scoparius, is a perennial leguminous shrub native to western and central Europe. In Britain and Ireland, the standard name is broom, but this name is also used for other members of the Genisteae tribe, such as French broom or Spanish broom, and the term common broom is sometimes used for clarification. In other English-speaking countries, the most prevalent common name is Scotch broom (or Scot's broom); English broom is also occasionally used.

Verio

Cytidine 5'-(tetrahydrogen triphosphate)

Cytochrome p-450 enzyme system

Cytogenetic map

Cyto

Cytochrome c nitrite reductase (ccNiR) (EC 1.7.2.2) is a bacterial enzyme that catalyzes the six electron reduction of nitrite to ammonia; an important step in the biological nitrogen cycle. The enzyme catalyses the second step in the two step conversion of nitrate to ammonia, which allows certain bacteria to use nitrite as a terminal electron acceptor, rather than oxygen, during anaerobic conditions. During this process, ccNiR draws electrons from the quinol pool, which are ultimately provided by a dehydrogenase such as formate dehydrogenase or hydrogenase. These dehydrogenases are responsible for generating a proton motive force.Cytochrome c Nitrite Reductase is a homodimer which contains five c-type heme cofactors per monomer. Four of the heme centers are bis-histidine ligated and presumably serve to shuttle electrons to the active site. The active site heme, however, is uniquely ligated by a single lysine residue.This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with a cytochrome as acceptor. The systematic name of this enzyme class is ammonia:ferricytochrome-c oxidoreductase.

Cytisophyllum sessilifolium is a species of flowering plants in the legume family, Fabaceae. It belongs to the subfamily Faboideae. It is the only member of the genus Cytisophyllum.

Cytochalasin b

Cytisopsis is a genus of flowering plants in the legume family, Fabaceae. It belongs to the sub family Faboideae.

Cytochrome c oxidase subunit I

CytoSport is an American Benicia, California manufacturer of sports-oriented nutritional products, or "supplements". It offers a line of protein-enhanced powders, shakes, and bars has broken into the mainstream market with a ready-to-drink form of protein supplement Muscle Milk, a non-dairy beverage which is trans-fat-free, lactose-free, contain no high fructose corn syrup and is shelf stable.

Species

Cytochrome c group

Cytogenetic and Genome Research is the name of a peer-reviewed scientific journal that was established in 1962. It was published previously under the names Cytogenetics (1962–1972) and Cytogenetics and Cell Genetics (1973–2001).

Ball-and-stick model of the cytisine molecule

Cytochromes

Cytidine deaminase is an enzyme that in humans is encoded by the CDA gene.This gene encodes an enzyme involved in pyrimidine salvaging. The encoded protein forms a homotetramer that catalyzes the irreversible hydrolytic deamination of cytidine and deoxycytidine to uridine and deoxyuridine, respectively. It is one of several deaminases responsible for maintaining the cellular pyrimidine pool. Mutations in this gene are associated with decreased sensitivity to the cytosine nucleoside analogue cytosine arabinoside used in the treatment of certain childhood leukemias.A related activation-induced (cytidine) deaminase (AID) regulates antibody diversification, especially the process of somatic hypermutation.

* Cytinus hypocistis subsp. hypocistis
* C. h. subsp. macranthus (Wettst.)
* C. h. subsp. orientalis (Wettst.)
* C. h. subsp. pityusensis (Finschow)
(List source:)

Cytochrome p450

Cytochrome C'
Cytochromes c (cytC) are electron-transfer proteins having one or several heme c groups, bound to the protein by one or, more generally, two thioether bonds involving sulphydryl groups of cysteine residues. The fifth haem iron ligand is always provided by a histidine residue. Cytochromes c possess a wide range of properties and function in a large number of different redox processes.

The enzyme cytochrome c oxidase or Complex IV, EC 1.9.3.1 is a large transmembrane protein complex found in bacteria and the mitochondrion of eukaryotes.It is the last enzyme in the respiratory electron transport chain of mitochondria (or bacteria) located in the mitochondrial (or bacterial) membrane. It receives an electron from each of four cytochrome c molecules, and transfers them to one oxygen molecule, converting molecular oxygen to two molecules of water.

Cyrus Griffin (July 16, 1749 – December 14, 1810) was a lawyer and judge who served as the last President of the Continental Congress, holding office from January 22, 1788, to November 2, 1788. He resigned after the ratification of the United States Constitution rendered the old Congress obsolete, and was later a United States federal judge.

Cytochalasins are fungal metabolites that have the ability to bind to actin filaments and block polymerization and the elongation of actin. As a result of the inhibition of actin polymerization, cytochalasins can change cellular morphology, inhibit cellular processes such as cell division, and even cause cells to undergo apoptosis. Cytochalasins have the ability to permeate cell membranes, prevent cellular translocation and cause cells to enucleate. Cytochalasins can also have an effect on other aspects of biological processes unrelated to actin polymerization. For example, cytochalasin A and cytochalasin B can also inhibit the transport of monosaccharides across the cell membrane, cytochalasin H has been found to regulate plant growth, cytochalasin D inhibits protein synthesis and cytochalasin E prevents angiogenesis.

Cytochrom_B_N

Cyto's Puzzle Adventure

Cytisus spachianus

Cytidine monophosphate, also known as 5'-cytidylic acid or simply cytidylate, and abbreviated CMP, is a nucleotide that is used as a monomer in RNA. It is an ester of phosphoric acid with the nucleoside cytidine. CMP consists of the phosphate group, the pentose sugar ribose, and the nucleobase cytosine; hence, a ribonucleoside monophosphate. As a substituent it takes the form of the prefix cytidylyl-.

Cytisine

Cytochrome c oxidase

Cytochrome c oxidase subunit 2, also known as cytochrome c oxidase polypeptide II, is a protein that in humans is encoded by the MT-CO2 gene.Cytochrome c oxidase subunit II, abbreviated COXII, COX2, COII, or MT-CO2, is the second subunit of cytochrome c oxidase.

Cyril Smith

Cytidine diphosphate diglycerides

Space-filling model of the cytidine triphosphate molecule as an anion

Cytochrome c nitrite reductase

cytochrome f from the b6f complex of Phormidium laminosum

Cytidine diphosphate glucose, often abbreviated CDP-glucose, is a nucleotide-linked sugar consisting of cytidine diphospahte and glucose.

Cytidine deaminase

UQCR4, MC3DN6

Cytochromes c1

CDP-glucose

Cytobands

Skeletal formula of cytidine diphosphate

CL0328

Ribbon diagram of erythrocytic methemoglobin reductase with FAD bound. From .

* Asarum hypocistis (L.)

Cyril Snedden

yes

Cytidine pyrophosphate

Cytochrophin-4 is an opioid peptide.

Judge of the United States District Court for the District of Virginia

Cytisus nigricans

Cyrtandra is a genus of flowering plants containing about 600 species, with more being discovered often, and is thus the largest genus in the family Gesneriaceae. These plants are native to Southeast Asia, Australia, and the Pacific Islands, with the centre of diversity in Southeast Asia and the Malesian region. The genus is common, but many species within it are very rare, localized, endangered endemic plants. The species can be difficult to identify because they are highly polymorphic and because they readily hybridize with each other. The plants may be small herbs, vines, shrubs, epiphytes, or trees. The genus is characterized in part by having two stamens, and most species have white flowers, with a few red-, orange-, yellow- and pink-flowered species known. Almost all species live in rainforest habitats.It is an example of a supertramp genus.Hawaiian Cyrtandra are known as ha‘iwale.Species include:Cyrtandra aurantiicarpaCyrtandra biserrata – Molokai cyrtandraCyrtandra calyptribracteataCyrtandra cleopatraeCyrtandra confertiflora – lava cyrtandraCyrtandra cordifolia – the Latin name means cyrtandra with heart-shaped leavesCyrtandra crenata – Kahana Valley cyrtandraCyrtandra cyaneoides – mapeleCyrtandra dentata – mountain cyrtandraCyrtandra elatostemoidesCyrtandra ferripilosa – red-hair cyrtandraCyrtandra filipes – gulch cyrtandraCyrtandra garnotiana – hahalaCyrtandra giffardii – forest cyrtandraCyrtandra gracilis – Palolo Valley cyrtandraCyrtandra grandiflora – largeflower cyrtandraCyrtandra grayana – Pacific cyrtandraCyrtandra grayi – Gray's cyrtandraCyrtandra halawensis – toothleaf cyrtandraCyrtandra hashimotoi – Maui cyrtandraCyrtandra hawaiensis – Hawaii cyrtandraCyrtandra hematos – singleflower cyrtandraCyrtandra hirtigeraCyrtandra hypochrysoidesCyrtandra kalihii – Koolau Range cyrtandraCyrtandra kamooloaensis – Kamo'oloa cyrtandraCyrtandra kauaiensis – ulunaheleCyrtandra kealiaeCyrtandra kealiae ssp. kealiae (syn. C. limahuliensis)Cyrtandra kealiae ssp. urceolataCyrtandra kohalae – Kohala Mountain cyrtandraCyrtandra laxiflora – Oahu cyrtandraCyrtandra lessoniana – Lesson's cyrtandraCyrtandra macraei – upland cyrtandraCyrtandra menziesii – ha'i waleCyrtandra munroi – Lanaihale cyrtandraCyrtandra nitensCyrtandra oenobarba – shaggystem cyrtandraCyrtandra olona – Kauai cyrtandraCyrtandra oxybapha – Pohakea Gulch cyrtandraCyrtandra paliku – cliffside cyrtandraCyrtandra paludosa – kanaweo ke'oke'oCyrtandra platyphylla – 'ilihiaCyrtandra polyantha – Niu Valley cyrtandraCyrtandra pruinosa – frosted cyrtandraCyrtandra pulgarensisCyrtandra samoensisCyrtandra sessilis – windyridge cyrtandraCyrtandra subumbellata – parasol cyrtandraCyrtandra tahuatensisCyrtandra tintinnabula – Laupahoehoe cyrtandraCyrtandra umbelliferaCyrtandra viridiflora – greenleaf cyrtandraCyrtandra waiolani – fuzzyflower cyrtandraCyrtandra wawrae – rockface cyrtandra

http://www.cricketarchive.com/Archive/Players/16/16706/16706.html CricketArchive

Cyril Smith (footballer)

http://www.espncricinfo.com/ci/content/player/38524.html Cricinfo

Cytochrome c oxidase, subunit Vb is a subunit of mitochondrial cytochrome c oxidase complex.Cytochrome c oxidase (EC 1.9.3.1) is an oligomeric enzymatic complex which is a component of the respiratory chain complex and is involved in the transfer of electrons from cytochrome c to oxygen.

CL0317

Cytisus platycarpos

Cytisus sessilifolius

Cytochrome C1

Cytochrome c oxidase subunit 3 is an enzyme that in humans is encoded by the MT-CO3 gene.Cytochrome c oxidase subunit III is one of main transmembrane subunits of cytochrome c oxidase.

The enzyme cytochrome c oxidase or Complex IV, EC 1.9.3.1 is a large transmembrane protein complex found in bacteria and the mitochondrion of eukaryotes.It is the last enzyme in the respiratory electron transport chain of mitochondria (or bacteria) located in the mitochondrial (or bacterial) membrane. It receives an electron from each of four cytochrome c molecules, and transfers them to one oxygen molecule, converting molecular oxygen to two molecules of water. In the process, it binds four protons from the inner aqueous phase to make water, and in addition translocates four protons across the membrane, helping to establish a transmembrane difference of proton electrochemical potential that the ATP synthase then uses to synthesize ATP.

Cytochrome f

(2S,3R)-2-(2S)-2-[[(2S)-1-[(2S)-2-Amino-3-(4-hydroxyphenyl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-phenylpropanoyl]amino]-3-hydroxybutanoic acid

Cytocuprein

In molecular biology, the cytochrome c assembly protein family includes various proteins involved in cytochrome c assembly from mitochondria and bacteria. Members of this family include: CycK from Rhizobium leguminosarum, CcmC from Escherichia coli and Paracoccus denitrificans, and orf240 from Triticum aestivum (Wheat) mitochondria.

Cytochrome bd-I oxidase

Cytochrome c reductase may refer to:Coenzyme Q – cytochrome c reductase, an enzymeNADH dehydrogenase, an enzyme

Cytochrom_C_2

CEO: Samuel M. Lawrence

Cytidine diphosphate choline

Cytochrome p-450 cyp2d6

sulfate respiration in desulfovibrio vulgaris hildenborough: structure of the 16-heme cytochrome c hmca at 2.5 a resolution and a view of its role in transmembrane electron transfer

Cytochrome bc1 complex

Cytochrophin

CGRYAJ

Plantae

Cytogenetic abnormality

Cyril Alexander Snedden

iOS: 8.2/10

Cytisaceae

Cyto-Stain, or CytoStain, is commercially available mix of staining dyes for polychromatic staining in histology. It provides results comparable to Papanicolaou staining, but in less number of operations and in shorter time. It is used in ultrafast Papanicolaou staining.Cyto-Stain G is a modification of Cyto-Stain, producing greener cyanophilic hues in intermediate and basal cells.[1]

Bacterial cytochrome c oxidase complex. Subunit II indicated by blue.

Cytochrome-b5 reductase (also known as methemoglobin reductase) is a NADH-dependent enzyme that converts methemoglobin to hemoglobin. It contains FAD and catalyzes the reaction:NADH + H+ + 2 ferricytochrome b5 = NAD+ + 2 ferrocytochrome b5The following four human genes encode cytochrome-b5 reductases:CYB5R1CYB5R2CYB5R3CYB5R4

Cytidine Triphosphate

Cytogenet. Genome Res.

Cytochrome b6

Cytogenetic analysis

Cytochrome bo oxidase

Cytochalasin D.png

Cyril Smith (pianist)

Cytidylic acid

Cyto Fluidics

Cytisus monspessulanus

Cyril James Smith OBE (11 August 1909 – 2 August 1974) was a virtuoso concert pianist of the 1930s, 1940s and 1950s, and a piano teacher.

Cytisus tinctoria

Cytochrom_C

Cytochrome P450 cinnamate 4-hydroxylase

Cyril C Smith

Chillingo

Auckland, New Zealand

Cytocanis

The Cytochrome b (-245) protein complex is composed of cytochrome b alpha (CYBA) and beta (CYBB) chain.

Cytogenetic

In enzymology, a cytidylate kinase (EC 2.7.4.14) is an enzyme that catalyzes the chemical reactionATP + (d)CMP ⇌ {\displaystyle \rightleftharpoons } ADP + (d)CDPThus, the two substrates of this enzyme are ATP and dCMP, whereas its two products are ADP and dCDP.This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor.

Cytogenetic studies

Cytisus caramanicus

Cytochrome c oxidase subunit III

Cytinium

Australia

Cytochrome C Oxidase

Cytisophyllum sessilifolium

Cyrus Griffin

Cyto's Puzzle Adventure is a casual physics based puzzle mobile game developed by Ukrainian game development studio Room 8. The game was first released on the iOS App Store on February 21, 2013. Later it was released on the other platforms:Mac App Store - October 22, 2013WildTangent PC - October 23, 2013WildTangent Android - December 19, 2013Android - December 19, 2013 Steam - July 13, 2014 Humble Store - October 23, 2014 On December 18, 2013, Room 8 Studio has changed the game's publisher to Kerosene Games.The game music was composed by Emmy-nominated Composer David Ari Leon.

Cytin

CytoViva, Inc. is a scientific imaging and instrumentation company that develops and markets optical microscopy and hyperspectral imaging technology for nanomaterials, pathogen and general biology applications.

TouchArcade

crystal structure of cytochrome c nitrite reductase nrfha complex from desulfovibrio vulgaris

Cytochrome P450 1A1

Cyto's Puzzle Adventure is a casual physics based puzzle mobile game developed by Ukrainian game development studio Room 8. The game was first released on the iOS App Store on February 21, 2013.

Cytochrome b559 is an important component of Photosystem II.PSII is a multisubunit protein-pigment complex containing polypeptides both intrinsic and extrinsic to the photosynthetic membrane.

Jaub. & Spach

Cytochrome bd oxidase

Cytochrome-c

Class III cytochrome C family

Cytogenetics, Cytogenetics and Cell Genetics

Cytochrome P450 system

Cytir Mawr (also written as Cyttir Mawr) is a local nature reserve in Llandegfan, Anglesey, Wales.There are ponds and the area is rich in plant and wildlife. The reserve was once owned by Cardiff University but was handed back to Anglesey.

Cytohesin-2

Cytochrome c

cytidylate kinase

Cytochrom_B561

atomic structure of a cytochrome c' with an unusual ligand-controlled dimer dissociation at 1.8 angstroms resolution

Cytochrome C

Cytisopsis

Cytogenetic and Genome Research

CytoSport

Sophorine

Centennial, CO 80112

Cytidine 3':5'-monophosphate phosphodiesterase (cyclic CMP)

C. hypocistis growing under a bush in leaf litter, near Fréjus in the south of France

CTP chemical structure.png

Animalia

C. hirsutus

Cytochrome c peroxidase

Cytochrome c assembly protein family

Cytisus scoparius

Piano

Cytoarchitectonics

Cyril James Smith

Cytochrome P450 14a-demethylase

Cytochrome a3

Cytisus striatus

Cytoglobin

Cytochrome P-450meg

Aberdare Thursday

Cytisine 3D ball.png

Cytoglobin is the protein product of CYGB, a human and mammalian gene.Cytoglobin is a globin molecule ubiquitously expressed in all tissues and most notably utilized in marine mammals. It was discovered in 2001 and named cytoglobin in 2002. It is thought to protect against hypoxia. The predicted function of cytoglobin is the transfer of oxygen from arterial blood to the brain.

Cytochrome c oxidase subunit II, transmembrane domain

COX5B

Cytochrome b-245 light chain is a protein that in humans is encoded by the CYBA gene involved in superoxide production and phagocytosis.Cytochrome b is composed of a light chain (alpha) and a heavy chain (beta). This gene encodes the light, alpha subunit, which has been proposed as a primary component of the microbicidal oxidase system of phagocytes. Mutations in this gene are associated with autosomal recessive chronic granulomatous disease (CGD), which is characterized by the failure of activated phagocytes to generate superoxide, which is important for the microbicidal activity of these cells.

Cytidine diphosphate-choline (CDP-Choline)

Cytochrome b-245, alpha polypeptide

Cytisus scoparius, the common broom or Scotch broom, syn. Sarothamnus scoparius, is a perennial leguminous shrub native to western and central Europe. In Britain and Ireland, the standard name is broom, but this name is also used for other members of the Genisteae tribe, such as French broom or Spanish broom, and the term common broom is sometimes used for clarification.

Cytidine monophosphoacetylneuraminate-(alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide-alpha-2,6-sialyltransferase

Cytochrom_B559a

Cytisophyllum

Cytisus hirsutus

Cytochrome C1 (also known as Complex III subunit 4) is a protein encoded by the CYC1 gene. Cytochrome is a heme-containing subunit of the cytochrome b-c1 complex, which accepts electrons from Rieske protein and transfers electrons to cytochrome c in the mitochondrial respiratory chain. It is formed in the cytosol and targeted to the mitochondrial intermembrane space. Cytochrome c1 belongs to the cytochrome c family of proteins.

Cytochrome oxidase

Cytogenetics and Genome Research

Cytochalasin E, a member of the cytochalasin group, is an inhibitor of actin polymerization in blood platelets. It inhibits angiogenesis and tumor growth. Unlike cytochalasin A and cytochalasin B, it does not inhibit glucose transport.Because of its antiangiogenic effect, cytochalasin E is a potential drug for age-related macular degeneration, a kind of blindness caused by an abnormal proliferation of blood vessels in the eye.

CytoViva, Inc

cytidylate cyclase

Cyto-stain

Cytogenetic maps

Arthropoda

cytochrome-c3 hydrogenase

Cytochrome 750 Oxidase

Cytochrome-C oxidase

Online archive

Complex III subunit 4, Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit

cytochrome-b5 reductase

Cytochromes c (cytC) are electron-transfer proteins having one or several heme c groups, bound to the protein by one or, more generally, two thioether bonds involving sulphydryl groups of cysteine residues. The fifth haem iron ligand is always provided by a histidine residue. Cytochromes c possess a wide range of properties and function in a large number of different redox processes. The founding member of this family is mitochondrial cytochrome c.Ambler recognized four classes of cytC.Class I includes the low-spin soluble cytC of mitochondria and bacteria, with the haem-attachment site towards the N-terminus, and the sixth ligand provided by a methionine residue about 40 residues further on towards the C-terminus. On the basis of sequence similarity, class I cytC were further subdivided into five classes, IA to IE. Class IB includes the eukaryotic mitochondrial cytC and prokaryotic 'short' cyt c2 exemplified by Rhodopila globiformis cyt c2; class IA includes 'long' cyt c2, such as Rhodospirillum rubrum cyt c2 and Aquaspirillum itersonii cytc-550, which have several extra loops by comparison with class IB cytC.Class II includes the high-spin cytC' and a number of low-spin cytochromes, e.g. cyt c-556. The haem-attachment site is close to the C terminus. The cytC' are capable of binding such ligands as CO, NO or CN(-), albeit with rate and equilibrium constants 100 to 1,000,000-fold smaller than other high-spin haemoproteins. This, coupled with its relatively low redox potential, makes it unlikely that cytC' is a terminal oxidase. Thus cytC' probably functions as an electron transfer protein. The 3D structures of a number of cytC' have been determined. The molecule usually exists as a dimer, each monomer folding as a four-alpha-helix bundle incorporating a covalently-bound haem group at the core. The Chromatium vinosum cytC' exhibits dimer dissociation upon ligand binding.Class III comprises the low redox potential multiple haem cytochromes: cyt C7 (trihaem), C3 (tetrahaem), and high-molecular-weight cytC, HMC (hexadecahaem), with only 30-40 residues per haem group. The haem c groups, all bis-histidinyl coordinated, are structurally and functionally nonequivalent and present different redox potentials in the range 0 to -400 mV. The 3D structures of a number of cyt C3 proteins have been determined. The proteins consist of 4-5 alpha-helices and 2 beta-strands wrapped around a compact core of four non-parallel haems, which present a relatively high degree of exposure to the solvent. The overall protein architecture, haem plane orientations and iron-iron distances are highly conserved.Class IV includes complex proteins containing other prosthetic groups besides haem c, such as flavocytochromes c and cytochromes cd.^ Miki K, Sogabe S, Uno A, et al. (May 1994). "Application of an automatic molecular-replacement procedure to crystal structure analysis of cytochrome c2 from Rhodopseudomonas viridis". Acta Crystallogr. D. 50 (Pt 3): 271–5. doi:10.1107/S0907444993013952. PMID 15299438. ^ Moore GR, Pettigrew GW (1987). : –. ^ a b Ambler RP (1991). "Sequence variability in bacterial cytochromes c". Biochim. Biophys. Acta. 1058 (1): 42–47. doi:10.1016/S0005-2728(05)80266-X. PMID 1646017. ^ Kassner RJ (May 1991). "Ligand binding properties of cytochromes c'". Biochim. Biophys. Acta. 1058 (1): 8–12. doi:10.1016/s0005-2728(05)80257-9. PMID 1646027. ^ a b Moore GR (May 1991). "Bacterial 4-alpha-helical bundle cytochromes". Biochim. Biophys. Acta. 1058 (1): 38–41. doi:10.1016/s0005-2728(05)80265-8. PMID 1646016. ^ Ren Z, Meyer T, McRee DE (November 1993). "Atomic structure of a cytochrome c' with an unusual ligand-controlled dimer dissociation at 1.8 A resolution". J. Mol. Biol. 234 (2): 433–45. doi:10.1006/jmbi.1993.1597. PMID 8230224. ^ a b Coutinho IB, Xavier AV (1994). "Tetraheme cytochromes". Meth. Enzymol. 243: 119–40. doi:10.1016/0076-6879(94)43011-X. PMID 7830606.

Cytisine, also known as baptitoxine and sophorine, is an alkaloid that occurs naturally in several plant genera, such as Laburnum and Cytisus of the family Fabaceae. It has been used medically to help with smoking cessation. Its molecular structure has some similarity to that of nicotine and it has similar pharmacological effects. Like varenicline, cytisine is a partial agonist of nicotinic acetylcholine receptors (nAChRs). Cytisine has a short half-life of 4.8 hours, and is rapidly eliminated from the body. The use of cytisine for smoking cessation remains relatively unknown outside Eastern Europe.

Cytochrome-b(5) reductase

an unidentified species

Cytochrome c peroxidase, or CCP is a water-soluble heme-containing enzyme of the peroxidase family that takes reducing equivalents from cytochrome c and reduces hydrogen peroxide to water:CCP + H2O2 + 2 ferrocytochrome c + 2H+ → CCP + 2H2O + 2 ferricytochrome cCytochrome c peroxidase can react with hydroperoxides other than hydrogen peroxide, but the reaction rate is much slower than with hydrogen peroxide.It was first isolated from baker's yeast by R. A.

Cytochrome P-450

Cytochrome P-450 (P-45017alpha,lyase)

Cytochrome C nitrite reductase

CTP; Cytidine-5'-triphosphate; Cytidine 5'-

Cytochrome-c oxidase deficiency

Cytogenet Genome Res

Cytochrome-b

C. striatus

balls

CytoSorb

Cytochrome-b5 reductase

Structure of Photosystem II from Thermosynechococcus elongatus.

Cytochrophin-4

Cytochrome b561 is an integral membrane protein responsible for electron transport, binding two heme groups non-covalently. It is a family of ascorbate-dependent oxidoreductase enzymes.

Cytochalasin D

Cytisophyllum sessilifolius

Cytochrome b5, form A (gene name CYB5A), is a human microsomal cytochrome b5.Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. It has two isoforms produced by alternative splicing. Isoform 1 is bound to the cytoplasmic side of the endoplasmic reticulum. It has a C-terminal transmembrane alpha-helix. Isoform 2 was found in cytoplasm. Defects in CYB5A are the cause of type IV hereditary methemoglobinemia.

Cystignathus zebra

Cytochrome c6f complex

Cyril Robert Smith (1 November 1926 – 1 January 2009) was an Australian first-class cricketer who played Sheffield Shield cricket for Queensland. He also represented his state in Australian rules football.Smith, who played his football as a ruckman, had an imposing figure, standing two metres tall and weighing 100 kg. On the cricket field he was a fast-medium paceman, who opening the bowling, usually with Len Johnson. He played regularly in the Queensland Australian National Football League for Yeronga and in 1950 was picked in the state squad to go to the Brisbane Carnival, only to withdraw with an injury.The Queenslander made his first-class cricket debut in the 1946/47 season, against the touring Indian team, but failed to pick up a wicket. He went for 75 runs in the first innings and then 42 from just five overs in the second. Another opportunity came two years later and from then until 1953/54 he missed few matches for Queensland.In the 1951/52 Sheffield Shield season, Smith took 20 wickets at 28.65, the best return of his career. He had also taken his innings figures, 7-58, in a match against Victoria at the SCG. It was the first time in Sheffield Shield history that a Queensland bowler had taken Victorian wickets in one innings. The Victorians continued to see the best of Smith throughout his career, with his final tally showing 32 wickets at 23.34. He played another international side that season, with the West Indies in the country for a Test series. Although he only took two wickets, both of them were an opening batsman, Jeff Stollmeyer. Another Test batsman who Smith had success with over the course of his career was Sam Loxton, whom he dismissed five times in first-class cricket.He was invited by Footscray president, Con Weichart, to train with the Victorian Football League club in April 1952. Weichart had spotted Smith at the MCG, when he was playing a Shield match against Victoria, and was impressed by his agility. He trained with coach Charlie Sutton for two weeks but in the end decided to stay in Queensland. Footscray instead debuted ruckman Brian Gilmore in 1952, who would play in the club's first ever premiership in 1954.After returns of 19 wickets at 31.57 and 16 wickets in 35.37, over the next two Shield season, Smith wasn't picked again for Queensland. The selectors had needed to drop a bowler, in order to fit former New South Wales bowling all-rounder Ray Lindwall in the team, and Smith was the one to make way.

Cytochrome f is the largest subunit of cytochrome b6f complex (plastoquinol—plastocyanin reductase; EC 1.10.99.1). In its structure and functions, the cytochrome b6f complex bears extensive analogy to the cytochrome bc1 complex of mitochondria and photosynthetic purple bacteria. Cytochrome f (cyt f) plays a role analogous to that of cytochrome c1, in spite of their different structures.The 3D structure of Brassica rapa (Turnip) cyt f has been determined.

Cyril Robert Smith

Cytochalasin d

Cytochrome b559

Insecta

Cytochrome p-450 cyp1a2

IPR0011

Cytofluorimeter

Cytochrome P450 2E1

Cytochrome f/b6 complex

Nippon Telegraph and Telephone Communications

Cytidine 5'-phosphocholine

Cytochromes b6

Cytisus striatus is a species of flowering plant in the legume family known by the common names hairy-fruited broom, Portuguese broom, French broom and Spanish broom. This plant is native to the Iberian Peninsula.

Cytisus supranubius

Cytochrome C oxidase polypeptide I

Feb 21, 2013

COX2_TM

CYC1

Prokaryotic cytochrome b561

Cytob

Cytidine 5'-diphosphocholine

"Cox1" redirects here. Particularly in a medical context, this can also refer to cyclooxygenase-1 (COX-1).Cytochrome c oxidase I (COX1) also known as mitochondrially encoded cytochrome c oxidase I (MT-CO1) is a protein that in humans is encoded by the MT-CO1 gene. In other eukaryotes, the gene is called COX1, CO1, or COI. Cytochrome c oxidase I is the main subunit of the cytochrome c oxidase complex.

cytochrome-c peroxidase

Cytochrome B

Cytodeme

O. Lang

Cytidine disphosphate

CL0105

Verio Inc.

Technology Development Director: James M. Beach Ph.D

Cytochrom_C_asm

Mitochondrial cytochrome bc1 complex

Cytidine-5'-triphosphate

Cytochemistry is the biochemistry of cells, especially that of the macromolecules responsible for cell structure and function. The term is also used to describe a process of identification of the biochemical content of cells.

Cytidine aminohydrolase

International

Cytisopsis dorycniifolia

Cytochrome P450 2C9

Cyril Snedden (7 September 1893 – 16 January 1985) was a New Zealand cricketer. He played four first-class matches for Auckland in 1920/21.

Cytisus battandieri

In enzymology, a cytidylate cyclase (EC 4.6.1.6) is an enzyme that catalyzes the chemical reactionCTP ⇌ {\displaystyle \rightleftharpoons } 3',5'-cyclic CMP + diphosphateHence, this enzyme has one substrate, CTP, and two products, 3',5'-cyclic CMP and diphosphate.This enzyme belongs to the family of lyases, specifically the class of phosphorus-oxygen lyases. The systematic name of this enzyme class is CTP diphosphate-lyase (cyclizing; 3',5'-cyclic-CMP-forming). Other names in common use include 3',5'-cyclic-CMP synthase, cytidylyl cyclase, cytidyl cyclase, and CTP diphosphate-lyase (cyclizing).

Cytidine 5'triphosphate

Cytochrome c oxidase subunit II

Cytoblast

Link

Cyto-Stain

Cyrtandra is a genus of flowering plants containing about 600 species, with more being discovered often, and is thus the largest genus in the family Gesneriaceae. These plants are native to Southeast Asia, Australia, and the Pacific Islands, with the centre of diversity in Southeast Asia and the Malesian region. The genus is common, but many species within it are very rare, localized, endangered endemic plants.

Cytochrom_CIII

Cytogenetics and Cell Genetics

Cytochrome C oxidase subunit II, periplasmic domain

Cytisus multiflorus is a species of legume known by the common names white broom and white spanishbroom.

Cytisus canariensis

CytoSport is an American Benicia, California manufacturer of sports-oriented nutritional products, or "supplements". It offers a line of protein-enhanced powders, shakes, and bars has broken into the mainstream market with a ready-to-drink form of protein supplement Muscle Milk, a non-dairy beverage which is trans-fat-free, lactose-free, contain no high fructose corn syrup and is shelf stable. Muscle Milk mainly markets on taste by using familiar milkshake flavors such as banana, milk chocolate and vanilla to drive consumers to the product, along with multiple drink sizes and formats, including powders and being sold in convenience stores alongside regular energy drinks and sports drinks.CytoSport was founded in 1998 by the father/son team of Greg and Mike Pickett. It produces its powder products and pre-blends of ready-to-drink products at a 150,000-square-foot (14,000 m2) manufacturing facility.Its products are endorsed by Pro-Bowl Running Back Adrian Peterson, and by Mike Bottom, the head coach of the University of Michigan men’s swimming program and former co-head men's swimming coach at the University of California, Berkeley.TSG Consumer Partners has financed Cytosport. The company reportedly earned US$200 million in 2008, and received the Small Company of the Year Award at the 16th annual Beverage Forum presented by Beverage World magazine and Beverage Marketing Corporation. Hormel announced it was acquiring CytoSport for $450 million in 2014.

Cytochrome p-450 cyp2e1

Cytochrome P450 3A4

Skeletal formula of cytidine triphosphate as an anion

Cytochrome P450 family

Cytochrome P450 eryF

Cytisus hirsutus (clustered broom or hairy broom) is a perennial plant belonging to the genus Cytisus of the Fabaceae family.

Cytochrome C assembly protein

Ni_hydr_CYTB

Cytobolin

Office abolished

VP, Sales & Marketing: Byron J. Cheatham

The following table summarizes symbols and abbreviations used in cytogenetics:

Cytidine diphosphate anion 3D spacefill.png

Cytinus hypocistis

Cytochrome bb3 oxidase

Vandal

In enzymology, a cytochrome-c3 hydrogenase (EC 1.12.2.1) is an enzyme that catalyzes the chemical reaction2 H2 + ferricytochrome c3 ⇌ {\displaystyle \rightleftharpoons } 4 H+ + ferrocytochrome c3Thus, the two substrates of this enzyme are H2 and ferricytochrome c3, whereas its two products are H+ and ferrocytochrome c3.This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with a cytochrome as acceptor. The systematic name of this enzyme class is hydrogen:ferricytochrome-c3 oxidoreductase. Other names in common use include H2:ferricytochrome c3 oxidoreductase, cytochrome c3 reductase, cytochrome hydrogenase, and hydrogenase [ambiguous]. It has 3 cofactors: iron, Nickel, and Iron-sulfur.

Cytochrome c oxidase, subunit Vb is a subunit of mitochondrial cytochrome c oxidase complex.Cytochrome c oxidase (EC 1.9.3.1) is an oligomeric enzymatic complex which is a component of the respiratory chain complex and is involved in the transfer of electrons from cytochrome c to oxygen. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasma membrane.In eukaryotes, in addition to the three large subunits, I, II and III, that form the catalytic centre of the enzyme complex, there are a variable number of small polypeptidic subunits. One of these subunits is known as Vb in mammals, V in Dictyostelium discoideum (Slime mold) and IV in yeast, binds a zinc atom. The sequence of subunit Vb is well conserved and includes three conserved cysteines that coordinate the zinc ion. Two of these cysteines are clustered in the C-terminal section of the subunit.

(2R,3S,4R,5R)-5-(4-amino-2-oxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl] hydrogenphosphate

Cytidylate

Cytisis

Lumenal portion of Cytochrome b559, alpha subunit

Cyrtandra (plant)

Skeletal formula of cytisine

Cytinus

CytoJournal

Cytochrome P450 2D6

[-5--3,4-dihydroxyoxolan-2-yl]methylhydrogen phosphate

Eukaryotic cytochrome b561

Cytidine 5'-diphosphate

Cytogeneticist

COX2

Cytochemistry

Cyril C Smith was a Welsh professional football inside left who played in the Football League for Charlton Athletic.

In enzymology, a cytochrome-c3 hydrogenase (EC 1.12.2.1) is an enzyme that catalyzes the chemical reaction2 H2 + ferricytochrome c3 ⇌ {\displaystyle \rightleftharpoons } 4 H+ + ferrocytochrome c3Thus, the two substrates of this enzyme are H2 and ferricytochrome c3, whereas its two products are H+ and ferrocytochrome c3.This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with a cytochrome as acceptor.

Cytiole

Cytidindiphosphat protoniert.svg

Cytochrome C oxidase subunit II

Baptitoxine

Cytochrome c Nitrite Reductase

hairy pods

Cytidine diphosphate, abbreviated CDP, is a nucleoside diphosphate. It is an ester of pyrophosphoric acid with the nucleoside cytidine. CDP consists of the pyrophosphate group, the pentose sugar ribose, and the nucleobase cytosine.

East Sheen, London, England

Cyril Robert Smith (1 November 1926 – 1 January 2009) was an Australian first-class cricketer who played Sheffield Shield cricket for Queensland. He also represented his state in Australian rules football.Smith, who played his football as a ruckman, had an imposing figure, standing two metres tall and weighing 100 kg. On the cricket field he was a fast-medium paceman, who opening the bowling, usually with Len Johnson.

Cytidine deaminase is an enzyme that in humans is encoded by the CDA gene.This gene encodes an enzyme involved in pyrimidine salvaging. The encoded protein forms a homotetramer that catalyzes the irreversible hydrolytic deamination of cytidine and deoxycytidine to uridine and deoxyuridine, respectively. It is one of several deaminases responsible for maintaining the cellular pyrimidine pool.

Cytochrome C oxidase deficiency

Cyril Smith (disambiguation)

Space-filling model of the cytidine monophosphate molecule as anion

Cytochemistry is the biochemistry of cells, especially that of the macromolecules responsible for cell structure and function. The term is also used to describe a process of identification of the biochemical content of cells. Cytochemistry is a science of localizing chemical components of cells and cell organelles on thin histological sections by using several techniques like enzyme localization, micro-incineration, micro-spectrophotometry, radioautography, cryo-electron microscopy, X-ray microanalysis by energy-dispersive X-ray spectroscopy, immunohistochemistry and cytochemistry, etc.

Cytidylic acid; 5'-Cytidylic acid; Cytidine 5'-monophosphate; Cytidine 5'-phosphate; Cytidylate; 5'-CMP

* Cytisophyllum sessilifolius (L.) O. Lang)

[-5--3,4-dihydroxyoxolan-2-yl]methyl dihydrogen phosphate

Cytidine diphosphate

USA
COO: John O. Lawrence

Cytochromes f

CytoViva, Inc. Logo.png

Cytochrome P450 oxidase

C. sessilifolium

Cytochrome P450

Cytidine monophosphoacetylneuraminate-lactosylceramide sialyltransferase

CytoJournal is a peer-reviewed PubMed-indexed open access online scientific journal on cytology that publishes research articles and information related to all aspects of diagnostic cytopathology, including topics such as molecular cytopathology.

Cytochrome-c3 hydrogenase

Aberdare

Cytoarchitectonics of the cerebral cortex

Cytochrome p-450 cyp1a1

Cytochrome c oxidase subunit Vb

In enzymology, a cytidylate kinase (EC 2.7.4.14) is an enzyme that catalyzes the chemical reactionATP + (d)CMP ⇌ {\displaystyle \rightleftharpoons } ADP + (d)CDPThus, the two substrates of this enzyme are ATP and dCMP, whereas its two products are ADP and dCDP.This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:CMP phosphotransferase. Other names in common use include: deoxycytidylate kinase, deoxycytidylate kinase, CMP kinase, CTP:CMP phosphotransferase, dCMP kinase, deoxycytidine monophosphokinase, UMP-CMP kinase, ATP:UMP-CMP phosphotransferase, and pyrimidine nucleoside monophosphate kinase. This enzyme participates in pyrimidine metabolism.

Cytochrom_NNT

Cytochrome 450

Cytodeme first emerged as a printed word more than 60 years ago in a book by Heslop-Harrison. Discussing the Deme Terminology - he continued "cytodeme, a population differing in some distinctive cytological feature from others." More precisely the cytodeme may be defined as the total assembly of all those individuals/organisms that use an identical specific suite of chromosomes to carry their genes. In most cases the suite is composed of several pairs of homologous chromosomes with or without a pair of sex chromosomes. Since the only acceptable proof of the identity (homology) of chromosomes lies in their ability to pair fully from end to end during meiosis it follows that:In asexual taxa membership of a cytodeme can only be presumed on such evidence as visual similarity of chromosomal ideotype, but never proved.In sexual taxa all of the members of one cytodeme are fully intercompatible (within the limits of sex and other genetical constraints like self-incompatibility mechanisms) yielding the fertile progeny which proves their membership.As a general rule for most species all of its members are of the same cytodeme excepting only the infrequent aneuploid aberrants. However some species are known to include several chromosome races which must necessarily belong to different cytodemes. Although it is not intrinsic in the formal definition it is a matter of commom observation that members of different cytodemes are essentially cross-incompatible and any hybrids that do arise are usually highly infertile.

Cytidine triphosphate anion 3D spacefill.png

Apocytochr_F_C

Cytoarchitecture (Greek κύτος= "cell" + αρχιτεκτονική= "architecture"), also known as cytoarchitectonics, is the study of the cellular composition of the body's tissues under the microscope. Applied particularly to the study of the central nervous system, cytoarchitectonics is one of the ways to parse the brain, by obtaining sections of the brain and staining them with chemical agents that reveal how neurons are "stacked" into layers.The study of the parcellation of nerve fibers (primarily axons) into layers forms the subject of myeloarchitectonics (<Gk. μυελός=marrow + αρχιτεκτονική=architecture), an approach complementary to cytoarchitectonics.

Cyril Smith (cricketer)

Cyrus Griffin .svg

The crystal structure of bovine cytochrome c oxidase in a phospholipid bilayer. The intermembrane space lies to top of the image. Adapted from

Cytidine diphosphate glucose

Cytocanis is a genus of moths of the Noctuidae family.

Cytogenet. Cell Genet.

Cytogenetics

Cyrus Grey Luce

[(2R,3S,4R,5R)-5-(4-Amino-2-oxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl dihydrogen phosphate

Cytochalasin

In molecular biology, the cytochrome c assembly protein family includes various proteins involved in cytochrome c assembly from mitochondria and bacteria. Members of this family include: CycK from Rhizobium leguminosarum, CcmC from Escherichia coli and Paracoccus denitrificans, and orf240 from Triticum aestivum (Wheat) mitochondria. The members of this family are probably integral membrane proteins with six predicted transmembrane helices that may comprise the membrane component of an ABC (ATP binding cassette) transporter complex. This transporter may be necessary for transport of some component needed for cytochrome c assembly. One member, R. leguminosarum CycK, contains a putative haem-binding motif. Wheat orf240 also contains a putative haem-binding motif and is a proposed ABC transporter with c-type haem as its proposed substrate. However it seems unlikely that all members of this family transport haem or c-type apocytochromes because P. denitrificans CcmC transports neither.

Cytodeme first emerged as a printed word more than 60 years ago in a book by Heslop-Harrison. Discussing the Deme Terminology - he continued "cytodeme, a population differing in some distinctive cytological feature from others." More precisely the cytodeme may be defined as the total assembly of all those individuals/organisms that use an identical specific suite of chromosomes to carry their genes.

CytoJournal is a peer-reviewed PubMed-indexed open access online scientific journal on cytology that publishes research articles and information related to all aspects of diagnostic cytopathology, including topics such as molecular cytopathology. It is owned and supported by a non-profit organization (Cytopathology Foundation Inc, USA).Broad areas of cytopathology covered include fine needle aspiration biopsy, Pap test (including Anal Pap), and serous fluids.The journal was established in July 2004 and was published initially by BioMed Central. The Cytopathology Foundation moved it to a new platform in July 2008 and it is currently published by Medknow Publications. The founding editors-in-chief were Vinod B. Shidham (Medical College of Wisconsin) and Barbara F. Atkinson (Kansas University Medical Center). Atkinson has retired and continues as editor-emeritus. The current editors-in chief are Richard M. Demay, Martha B. Pitman, and Vinod B. Shidham. In 2014 the journal had its impact factor suppressed due to anomalous self-citation patterns.

Cytochrome P450 CYP51 14α-demethylase

Cytidine monophosphate

Cytoarchitecture

iOS: 71%

Cytidine monophosphate anion 3D spacefill.png

Cytoarchitecture (Greek κύτος= "cell" + αρχιτεκτονική= "architecture"), also known as cytoarchitectonics, is the study of the cellular composition of the body's tissues under the microscope.

Cytochromes P450 (CYPs) are proteins of the superfamily containing heme as a cofactor and, therefore, are hemoproteins. CYPs use a variety of small and large molecules as substrates in enzymatic reactions. They are, in general, the terminal oxidase enzymes in electron transfer chains, broadly categorized as P450-containing systems.

Cytochalasins are fungal metabolites that have the ability to bind to actin filaments and block polymerization and the elongation of actin. As a result of the inhibition of actin polymerization, cytochalasins can change cellular morphology, inhibit cellular processes such as cell division, and even cause cells to undergo apoptosis. Cytochalasins have the ability to permeate cell membranes, prevent cellular translocation and cause cells to enucleate.

Cytochrome P450 enzyme system

Cytidine triphosphate is a pyrimidine nucleoside triphosphate.CTP, much like ATP, consists of a ribose sugar, and three phosphate groups. The major difference between the two molecules is the base used, which in CTP is cytosine.CTP is a substrate in the synthesis of RNA.CTP is a high-energy molecule similar to ATP, but its role as an energy coupler is limited to a much smaller subset of metabolic reactions.

Cytochrome b5, type A

Cytochrome c reductase

iOS: 75/100

Cytochrome b561

Cytisus weldenii

Cytisus multiflorus

Cytochrome P450 14α-demethylase

Cytogenetic notation

Game icon

Cytochromes P450 (CYPs) are proteins of the superfamily containing heme as a cofactor and, therefore, are hemoproteins. CYPs use a variety of small and large molecules as substrates in enzymatic reactions. They are, in general, the terminal oxidase enzymes in electron transfer chains, broadly categorized as P450-containing systems. The term P450 is derived from the spectrophotometric peak at the wavelength of the absorption maximum of the enzyme (450 nm) when it is in the reduced state and complexed with carbon monoxide.CYP enzymes have been identified in all kingdoms of life: animals, plants, fungi, protists, bacteria, archaea, and even in viruses. However, they are not omnipresent; for example, they have not been found in Escherichia coli. More than 200,000 distinct CYP proteins are known.Most CYPs require a protein partner to deliver one or more electrons to reduce the iron (and eventually molecular oxygen). Based on the nature of the electron transfer proteins, CYPs can be classified into several groups:Microsomal P450 systems, in which electrons are transferred from NADPH via cytochrome P450 reductase (variously CPR, POR, or CYPOR). Cytochrome b5 (cyb5) can also contribute reducing power to this system after being reduced by cytochrome b5 reductase (CYB5R).Mitochondrial P450 systems, which employ adrenodoxin reductase and adrenodoxin to transfer electrons from NADPH to P450.Bacterial P450 systems, which employ a ferredoxin reductase and a ferredoxin to transfer electrons to P450.CYB5R/cyb5/P450 systems, in which both electrons required by the CYP come from cytochrome b5.FMN/Fd/P450 systems, originally found in Rhodococcus species, in which a FMN-domain-containing reductase is fused to the CYP.P450 only systems, which do not require external reducing power. Notable ones include thromboxane synthase (CYP5), prostacyclin synthase (CYP8), and CYP74A (allene oxide synthase).The most common reaction catalyzed by cytochromes P450 is a monooxygenase reaction, e.g., insertion of one atom of oxygen into the aliphatic position of an organic substrate (RH) while the other oxygen atom is reduced to water:RH + O2 + NADPH + H+ → ROH + H2O + NADP+Many hydroxylation reactions (insertion of hydroxyl groups) use CYP enzymes.

The cytochrome complex, or cyt c is a small hemeprotein found loosely associated with the inner membrane of the mitochondrion. It belongs to the cytochrome c family of proteins. Cytochrome c is highly water-soluble, unlike other cytochromes, and is an essential component of the electron transport chain, where it carries one electron. It is capable of undergoing oxidation and reduction, but does not bind oxygen. It transfers electrons between Complexes III (Coenzyme Q – Cyt C reductase) and IV (Cyt C oxidase). In humans, cytochrome c is encoded by the CYCS gene.

Cystignathus hidalgoi

Cytochrome f is the largest subunit of cytochrome b6f complex (plastoquinol—plastocyanin reductase; EC 1.10.99.1). In its structure and functions, the cytochrome b6f complex bears extensive analogy to the cytochrome bc1 complex of mitochondria and photosynthetic purple bacteria. Cytochrome f (cyt f) plays a role analogous to that of cytochrome c1, in spite of their different structures.The 3D structure of Brassica rapa (Turnip) cyt f has been determined. The lumen-side segment of cyt f includes two structural domains: a small one above a larger one that, in turn, is on top of the attachment to the membrane domain. The large domain consists of an anti-parallel beta-sandwich and a short haem-binding peptide, which form a three-layer structure. The small domain is inserted between beta-strands F and G of the large domain and is an all-beta domain. The haem nestles between two short helices at the N terminus of cyt f. Within the second helix is the sequence motif for the c-type cytochromes, CxxCH (residues 21-25), which is covalently attached to the haem through thioether bonds to Cys-21 and Cys-24. His-25 is the fifth haem iron ligand. The sixth haem iron ligand is the alpha-amino group of Tyr-1 in the first helix. Cyt f has an internal network of water molecules that may function as a proton wire. The water chain appears to be a conserved feature of cyt f.

non_vocal_instrumentalist

Sale, Victoria, Australia

Cytochrome b-245 light chain is a protein that in humans is encoded by the CYBA gene involved in superoxide production and phagocytosis.Cytochrome b is composed of a light chain (alpha) and a heavy chain (beta). This gene encodes the light, alpha subunit, which has been proposed as a primary component of the microbicidal oxidase system of phagocytes.

Cyrtandra

[(2R,3S,4R,5R)-5-(4-amino-2-oxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl(hydroxy-phosphonooxyphosphoryl)hydrogen phosphate

Cytidylate kinase

Cytochrome b6f

Cytochalasins

Cytochrome c nitrite reductase (ccNiR) (EC 1.7.2.2) is a bacterial enzyme that catalyzes the six electron reduction of nitrite to ammonia; an important step in the biological nitrogen cycle. The enzyme catalyses the second step in the two step conversion of nitrate to ammonia, which allows certain bacteria to use nitrite as a terminal electron acceptor, rather than oxygen, during anaerobic conditions.

Cytochrome d is a protein that belongs to the Cytochrome family (electron-transporting proteins). Concretely, it is an enzyme – a protein that catalyses a chemical reaction. Cytochrome d is also known as cytochrome/heme a2. It is found in plenty of aerobic bacteria, especially when it has grown with a limited oxygen supply. The bacteria species in which it is more commonly found are Escherichia coli and Aerobacter aerogenes.

Cytochrome b5 reductase

Cytiseae

Cytochrome c peroxidase, or CCP is a water-soluble heme-containing enzyme of the peroxidase family that takes reducing equivalents from cytochrome c and reduces hydrogen peroxide to water:CCP + H2O2 + 2 ferrocytochrome c + 2H+ → CCP + 2H2O + 2 ferricytochrome cCytochrome c peroxidase can react with hydroperoxides other than hydrogen peroxide, but the reaction rate is much slower than with hydrogen peroxide.It was first isolated from baker's yeast by R. A. Altschul, Abrams, and Hogness in 1940, though not to purity. The first purified preparation of yeast CCP dates to Takashi Yonetani and his preparation by ion exchange chromatography in the early 1960s. The X-ray structure was the work of Thomas Poulos and coworkers in the late 1970s.The yeast enzyme is a monomer of molecular weight 34,000, containing 293 amino acids, and contains as well a single noncovalently bound heme b. Unusual for proteins, this enzyme crystallizes when dialysed against distilled water. More so, the enzyme purifies as a consequence of crystallization, making cycles of crystallization an effective final purification step.Much like catalase, the reaction of cytochrome c peroxidase proceeds through a three-step process, forming first a Compound I and then a Compound II intermediate:CCP + ROOH → Compound I + ROH + H2OCCP-compound I + e− + H+ → Compound IICompound II + e− + H+ → CCPCCP in the resting state has a ferric heme, and, after the addition of two oxidizing equivalents from a hydroperoxide (usually hydrogen peroxide), it becomes oxidised to a formal oxidation state of +5 (FeV, commonly referred to as ferryl heme However, both low-temperature magnetic susceptibility measurements and Mössbauer spectroscopy show that the iron in Compound I of CCP is a +4 ferryl iron, with the second oxidising equivalent existing as a long-lived free-radical on the side-chain of the tryptophan residue (Trp-191). This is different to most peroxidases, which have the second oxidising equivalent on the porphyrin instead. Compound I of CCP is fairly long-lived, decaying to CCP-compound II with a half-life at room temperature of 40 minutes to a couple hours.CCP has high sequence identity to the closely-related ascorbate peroxidase enzyme.

New Position

Cytogenetic localization

Knighton, Wales

* Cytisophyllum sessilifolius ( O. Lang)
* Cytisus sessilifolius (L.)

Cytochalasin E.png

Cytochrome P-45017alpha

M. Schmid

Royal Welsh Fusiliers

Cytochrome b

Cytochrome P450 90C1

Cytochrome P450 158A2

Cytisine, also known as baptitoxine and sophorine, is an alkaloid that occurs naturally in several plant genera, such as Laburnum and Cytisus of the family Fabaceae. It has been used medically to help with smoking cessation. Its molecular structure has some similarity to that of nicotine and it has similar pharmacological effects. Like varenicline, cytisine is a partial agonist of nicotinic acetylcholine receptors (nAChRs).

Cytidylate cyclase

Cytochrom_B559

Crystallographic structure of a homodimer of the cytochrome c nitrite reductase from Escherichia coli complexed with heme C .

Cytochrophin; Tyr-Pro-Phe-Thr; (L)-Tyrosyl-(L)-prolyl-(L)-phenylalanyl-(L)-threonine

Cytochrome P450meg

Structure of cytochrome c2 from Rhodopseudomonas viridis.

Slide to Play

Cytochrome-c peroxidase

Cytochrome b559 is an important component of Photosystem II.PSII is a multisubunit protein-pigment complex containing polypeptides both intrinsic and extrinsic to the photosynthetic membrane. Within the core of the complex, the chlorophyll and beta-carotene pigments are mainly bound to the antenna proteins CP43 (PsbC) and CP47 (PsbB), which pass the excitation energy on to chlorophylls in the reaction centre proteins D1 (Qb, PsbA) and D2 (Qa, PsbD) that bind all the redox-active cofactors involved in the energy conversion process. The PSII oxygen-evolving complex (OEC) provides electrons to re-reduce the PSII reaction center and oxidizes 2 water molecules to recover its reduced initial state. It consists of OEE1 (PsbO), OEE2 (PsbP) and OEE3 (PsbQ). The remaining subunits in PSII are of low molecular weight (less than 10 kDa), and are involved in PSII assembly, stabilisation, dimerisation, and photo-protection.Cytochrome b559, which forms part of the reaction centre core of PSII is a heterodimer composed of one alpha subunit (PsbE), one beta (PsbF) subunit, and a heme cofactor. Two histidine residues from each subunit coordinate the haem. Although cytochrome b559 is a redox-active protein, it is unlikely to be involved in the primary electron transport in PSII due to its very slow photo-oxidation and photo-reduction kinetics. Instead, cytochrome b559 could participate in a secondary electron transport pathway that helps protect PSII from photo-damage. Cytochrome b559 is essential for PSII assembly.This domain occurs in both the alpha and beta subunits of cytochrome B559. In the alpha sbunit it occurs together with a lumenal domain (InterPro: IPR013082), while in the beta subunit it occurs on its own.Cytochrome b559 can exist in three forms, each with a characteristic redox potential, These forms are very low potential (VLP), ≤ zero mV; low potential (LP) at 60 mV; and high potential (HP) at 370 mV. There is also an intermediate potential (IP) form that has a redox potential at pH 6.5-7.0 that ranges from 170 to 240 mV. In oxygen evolving reaction centers, more than half of the cyt b559 is in the HP form. In manganese depleted non oxygen evolving photosystem II reaction centers, cyt b559 is usually in the LP form.

Cytisus patens

Cytochrome P450 monooxygenase

Cytochalasin E

C. scoparius

Cytogenesis

Cytidine triphosphate is a pyrimidine nucleoside triphosphate.CTP, much like ATP, consists of a ribose sugar, and three phosphate groups. The major difference between the two molecules is the base used, which in CTP is cytosine.CTP is a substrate in the synthesis of RNA.CTP is a high-energy molecule similar to ATP, but its role as an energy coupler is limited to a much smaller subset of metabolic reactions. CTP is a coenzyme in metabolic reactions like the synthesis of glycerophospholipids and glycosylation of proteins.CTP acts as an inhibitor of the enzyme Aspartate carbamoyltransferase, which is used in pyrimidine biosynthesis.

Cytochrome b-245

Cytochrome P450 monooxygenase system

C. hypocistis

Auburn, AL

Rothm.

Cytochrome aa3-600 oxidase

Cytojournal

Cytochrome a

Cytidylyl

This gene encodes an enzyme involved in pyrimidine salvaging. The encoded protein forms a homotetramer that catalyzes the irreversible hydrolytic deamination of cytidine and deoxycytidine to uridine and deoxyuridine, respectively. It is one of several deaminases responsible for maintaining the cellular pyrimidine pool. Mutations in this gene are associated with decreased sensitivity to the cytosine nucleoside analogue cytosine arabinoside used in the treatment of certain childhood leukemias.

Cytogenet Cell Genet

Skeletal formula of cytidine monophosphate as an anion

Cytogenetic abnormalities

Structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus.

Cytocentrum

C. multiflorus

Cytochrome c family