A cooperative model for protonmotive heme-copper oxidases.: The role of heme a in the proton pump of cytochrome c oxidase

被引：39
|
作者：
Papa, S [1 ]
Capitanio, N [1 ]
Villani, G [1 ]
机构：
[1] Univ Bari, Inst Med Biochem & Chem, I-70124 Bari, Italy
来源：
FEBS LETTERS | 1998年 / 439卷 / 1-2期
关键词：
cytochrome c oxidase; proton pump; cooperative coupling;
D O I：
10.1016/S0014-5793(98)01305-2
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Oxide-reductions of metal centers in cytochrome c oxidase are linked to pK shifts of acidic groups in the enzyme (redox Bohr effects). The linkage at heme a results in proton uptake from the inner space upon reduction and proton release in the external space upon oxidation of the metal. The relationship of this process to the features of the proton pump in cytochrome c oxidase and its atomic structure revealed by X-ray crystallography to 2.8-2.3 Angstrom resolution is examined. A mechanism for the proton pump of cytochrome c oxidase, based on cooperative coupling at heme a, is proposed. (C) 1998 Federation of European Biochemical Societies.
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页码：1 / 8
页数：8
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