| UQCRC | ubiquinol-cytochrome C reductase core |
|---|---|
| CCO | cytochrome C oxidase |
| COX | cytochrome c oxidase |
| CYC | cyclophosphamide; cytochrome C |
| CYT | cytochrome |
| cytochrome a,a3 | cytochrome oxidase |
|---|---|
| CPR | NADPH--cytochrome P450 reductase |
| HMG-CoA reductase | 3-Hydroxy-3-methylglutaryl CoA reductase |
| HMG-CoA reductase | 3-Hydroxy-3-methylglutaryl coenzyme A reductase |
| CYP | cytochrome P |
| QH2 cytochrome C reductase | <enzyme> Membrane bound complex in the mitochondrial inner membrane, responsible for electron transfer from reduced coenzyme Q to cytochrome C. Contains cytochromes b and c1 and iron sulphur proteins. (18 Nov 1997) |
|---|
| core II protein, ubiquinol-cytochrome c reductase | <chemical> Member of the mitochondrial-protein-processing family; protein found in subunits of ubiquinol-cytochrome c reductase; amino acid sequence given in first source Synonym: core II protein, uccreductase (26 Jun 1999) |
|---|---|
| core I protein, ubiquinol-cytochrome c reductase | <chemical> Member of the mitochondrial-protein-processing family; protein found in subunits of ubiquinol-cytochrome c reductase; amino acid sequence given in first source Synonym: core I protein, uccreductase (26 Jun 1999) |
| cytochrome b5 reductase | <enzyme> An enzyme catalyzing the reduction of 2ferricytochrome b5 to 2ferrocytochrome b5 at the expense of NADH; has a role in fatty acid desaturation; a deficiency can lead to hereditary methemoglobinaemia (type I, only observed in erythrocyte cytosol; type II, deficiency in all tissues; type III, deficiency in all haematopoetic cells). (05 Mar 2000) |
| cytochrome b(5) reductase | <enzyme> May be the enzyme for methemoglobin reductase activity Registry number: EC 1.6.2.2 Synonym: NADH-cytochrome b5 reductase, mcr1 protein, saccharomyces cerevisiae, mcr1 gene product (26 Jun 1999) |
| cytochrome c2 reductase | <enzyme> An enzyme catalyzing the reduction of 2 ferricytochrome c2 to 2 ferrocytochrome c2 at the expense of NADPH. Synonym: cytochrome c2 reductase. (05 Mar 2000) |
| cytochrome c reductase | <enzyme> A flavoprotein containing iron. Cytochrome c may act as receptor. The enzyme reversibly catalyses the oxidation of NADH to NAD and reduced acceptor. An inherited deficiency of this complex results in overwhelming acidosis. Synonym: cytochrome c reductase. Chemical name: NADH:(acceptor) oxidoreductase Registry number: EC 1.6.99.3 (12 Dec 1998) |
| cytochrome reductase | <enzyme> A flavoprotein that catalyses the reduction of haem-thiolate-dependent monooxygenases and is part of the microsomal hydroxylating system. Its physiological acceptor is probably cytochrome p-450. Chemical name: NADPH:ferrihemoprotein oxidoreductase Registry number: EC 1.6.2.4 (12 Dec 1998) |
| NADH-cytochrome P-450 reductase | <enzyme> A component of the cytochrome p-450sca monoxygenase system Registry number: EC 1.6.2.- (26 Jun 1999) |
| NADPH-cytochrome c2 reductase | <enzyme> An enzyme catalyzing the reduction of 2 ferricytochrome c2 to 2 ferrocytochrome c2 at the expense of NADPH. Synonym: cytochrome c2 reductase. (05 Mar 2000) |
| ubiquinol-cytochrome-c reductase | <enzyme> An 11-subunit enzyme complex that acts as an electron transferring protein in the mitochondrial respiratory chain. The enzyme complex catalyses the oxidation of ubiquinol to ubiquinone and ferrocytochrome c in the presence of ferricytochrome c. It contains cytochromes b-562, b-566, and c1 as well as an iron ferredoxin. Chemical name: Ubiquinol-ferricytochrome-c oxidoreductase Registry number: EC 1.10.2.2 (12 Dec 1998) |
| porphyrin cytochrome c peroxidase | <enzyme> From yeast; haem group of cytochrome c peroxidase (EC 1.11.1.5) replaced by protoporphyrin ix Registry number: EC 1.11.1.- Synonym: pcc-peroxidase (26 Jun 1999) |
| cytochrome | <biochemistry> Any electron transfer haemoprotein having a mode of action in which the transfer of a single electron is effected by a reversible valence change of the central iron atom of the haem prosthetic group between the +2 and +3 oxidation states. Classified as cytochromes a in which the haem contains a formyl side chain, cytochromes b, which contain protohaem or a closely similar haem that is not covalently bound to the protein, cytochromes C in which protohaem or other haem is covalently bound to the protein and cytochromes d in which the iron tetrapyrrole has fewer conjugated double bonds than the haems have. Well known cytochromes have been numbered consecutively within groups and are designated by subscripts (beginning with no subscript), for example cytochromes C, c1, C2,. New cytochromes are named according to the wavelength in nanometres of the absorption maximum of the a band of the iron (II) form in pyridine, for example, C 555. Origin: Gr. Chroma = colour (18 Nov 1997) |
| cytochrome a | <chemical> Cytochromes (electron-transporting proteins) in which the haem prosthetic group is haem a, i.e., the iron chelate of cytoporphyrin ix. Chemical name: Cytochrome a (12 Dec 1998) |
| cytochrome aa3 | <enzyme> An enzyme complex of the inner mitochondrial membrane that catalyses the reaction between ferrocytochrome c and oxygen to yield ferricytochrome c and water. It is associated with the pumping of protons and the resultant phosphorylation of ADP to ATP. The reaction is the terminal event in the electron transport scheme by which oxygen is used for fuel combustion. It is a part of Complex IV of the respiratory chain. A deficiency of one or more of the polypeptides of this complex results in neuronal loss in brain leading to psychomotor retardation and neurodegenerative disease. Synonym: cytochrome aa3, indophenol oxidase, indophenolase. Chemical name: Ferricytochrome-c:oxygen oxidoreductase Registry number: EC 1.9.3.1 (12 Dec 1998) |
| cytochrome b | <chemical> Cytochromes (electron-transporting proteins) with protoheme or a related haem as the prosthetic group. The prosthetic group is not covalently bound to the protein moiety. Chemical name: Cytochrome b (12 Dec 1998) |
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