Synonyms : Cytochrome Oxidase Deficiency, Deficiency, Cytochrome-c Oxidase, Cytochrome Oxidase Deficiencies, Cytochrome c Oxidase Deficiency, Cytochrome-c Oxidase Deficiencies, Deficiencies, Cytochrome Oxidase, Deficiencies, Cytochrome-c Oxidase
Synonyms : Cytochrome Peroxidase, Cytochrome c-551 Peroxidase, Cytochrome c 551 Peroxidase, Cytochrome c Peroxidase, Peroxidase, Cytochrome, Peroxidase, Cytochrome c-551, Peroxidase, Cytochrome-c
Synonyms : Cytochrome
Synonyms :
Synonyms : Cytochrome a(1), Cytochrome a-1, Cytochrome a1, Cytochrome a 1
| cytochrome oxidase |
cytochrome-c oxidase.
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| cytochrome-b |
[EC 1.6.2.2] an enzyme of the endoplasmic reticulum and erythrocytes that catalyzes several series of redox reactions transferring electrons from NADH to an acceptor via the intermediate electron carrier cytochrome b5. It is a flavoprotein (FAD). In the endoplasmic reticulum, the enzyme is composed of polar and hydrophobic segments and is membrane-bound; the reduced cytochrome b5 carries electrons in several reactions of fatty acid desaturation and fatty acid elongation. In the erythrocytes, the enzyme comprises the polar segment only and is soluble; the reduced cytochrome b5 transfers electrons to methemoglobin, reducing it to hemoglobin. Deficiency of the enzyme, an autosomal recessive trait, results in hereditary methemoglobinemia; deficiency in erythrocytes only is characterized by cyanosis whereas deficiency also in leukocytes, and sometimes brain and muscle, has been linked to both cyanosis and mental retardation. Called also NADH cytochrome-b5 reductase, NADH methemoglobin reductase, and methemoglobin reductase (NADH).
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| cytochrome-c |
[EC 1.9.3.1] an enzyme complex of the inner mitochondrial membrane that catalyzes the transfer of electrons from cytochrome c to oxygen, oxidizing the former and reducing the latter in the final step of the electron transport chain (q.v.) by which oxygen is used for fuel combustion. The enzyme contains cytochromes a and a3 and two copper atoms and is associated with proton translocation and the resultant synthesis of ATP. The Fe2+ in heme a has a strong affinity for CO; in the Fe3+ state it binds CN-, S2-, and N3. The binding of these compounds inactivates the enzyme, a cause of their extreme toxicity for all aerobic organisms. Called also cytochrome aa3 and cytochrome oxidase.
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| cytochrome P450 |
A group of enzymes present in every type of cell in the body except red blood cells and skeletal muscle cells. They are important in metabolizing substances normally present in the body such as steroids, fat-soluble vitamins, fat
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| cytochrome transport system |
The last stage in aerobic cell respiration. SYN: electron transport chain.
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