Current issues in the chemistry of cytochrome c oxidase.
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.
Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77251-1892.
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Palmer
D000818:Animals; D001386:Azides / Q000378:metabolism / Q000494:pharmacology; D001665:Binding Sites; D003300:Copper / Q000032:analysis; D003486:Cyanides / Q000378:metabolism / Q000494:pharmacology; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D006418:Heme / Q000737:chemistry / Q000378:metabolism; D008322:Mammals; D010084:Oxidation-Reduction; D019810:Sodium Azide
D001386:Azides; D003486:Cyanides; D006418:Heme; D003300:Copper; D019810:Sodium Azide; D003576:Electron Transport Complex IV