Descriptor English: | Cytochromes | ||||
Descriptor Spanish: |
Citocromos
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Descriptor Portuguese: | Citocromos | ||||
Descriptor French: | Cytochromes | ||||
Entry term(s): |
Cytochrome |
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Tree number(s): |
D08.244 D12.776.422.220 |
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RDF Unique Identifier: | https://id.nlm.nih.gov/mesh/D003580 | ||||
Scope note: | Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands. |
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Annotation: | general or unspecified; prefer specific cytochrome |
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Allowable Qualifiers: |
AD administration & dosage AE adverse effects AI antagonists & inhibitors AN analysis BI biosynthesis BL blood CF cerebrospinal fluid CH chemistry CL classification CS chemical synthesis DE drug effects DF deficiency EC economics GE genetics HI history IM immunology IP isolation & purification ME metabolism PD pharmacology PH physiology PK pharmacokinetics PO poisoning RE radiation effects SD supply & distribution ST standards TO toxicity TU therapeutic use UL ultrastructure UR urine |
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DeCS ID: | 3598 | ||||
Unique ID: | D003580 | ||||
NLM Classification: | WH 190 | ||||
Documents indexed in the Virtual Health Library (VHL): | Click here to access the VHL documents | ||||
Date Established: | 1966/01/01 | ||||
Date of Entry: | 1999/01/01 | ||||
Revision Date: | 2003/07/09 |
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CHEMICALS AND DRUGS
Enzymes and Coenzymes [D08]Enzymes and Coenzymes -
CHEMICALS AND DRUGS
Amino Acids, Peptides, and Proteins [D12]Amino Acids, Peptides, and Proteins
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Cytochromes
- Preferred
Concept UI |
M0005598 |
Scope note | Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands. |
Preferred term | Cytochromes |
Entry term(s) |
Cytochrome |
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