Abstract
Some contemporary issues relevant to the chemistry of mammalian cytochrome c oxidase are discussed. These include the optical properties of heme A and the spectroscopic consequences of the differences in side-chain substitution compared to heme B; a common fallacy concerning the electrostatic exchange interaction between cytochrome a3 and CuB; the question of the number and location of the copper components of the enzyme; and the mode of binding of ligands such as cyanide and azide.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Animals
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Azides / metabolism
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Azides / pharmacology
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Binding Sites
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Copper / analysis
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Cyanides / metabolism
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Cyanides / pharmacology
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Electron Transport Complex IV / chemistry*
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Electron Transport Complex IV / isolation & purification
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Electron Transport Complex IV / metabolism
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Heme / chemistry
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Heme / metabolism
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Mammals
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Oxidation-Reduction
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Sodium Azide
Substances
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Azides
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Cyanides
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Heme
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Copper
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Sodium Azide
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Electron Transport Complex IV