Regulation of energy transduction and electron transfer in cytochrome c oxidase by adenine nucleotides

被引：25
|
作者：
Kadenbach, B [1 ]
Napiwotzki, J [1 ]
Frank, V [1 ]
Arnold, S [1 ]
Exner, S [1 ]
Hüttemann, M [1 ]
机构：
[1] Univ Marburg, Fachbereich Chem, D-35032 Marburg, Germany
来源：
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES | 1998年 / 30卷 / 01期
关键词：
cytochrome c oxidase; H+/e(-) stoichiometry; thermogenesis; adenine nucleotides; regulation of activity; ectotherm animals; ATP/ADP ratios; allosteric enzyme; monoclonal antibodies; rate of respiration;
D O I：
10.1023/A:1020599209468
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
Cytochrome c oxidase from bovine heart contains seven high-affinity binding sites for ATP or ADP and three additional only for ADP. One binding site for ATP or ADP, located at the matrix-oriented domain of the heart-type subunit VIaH, increases the H+/e(-) stoichiometry of the enzyme from heart or skeletal muscle from 0.5 to 1.0 when bound ATP is exchanged by ADP. Two further binding sites for ATP or ADP, located at the cytosolic and the matrix domain of subunit IV, increases the KM for cytochrome c and inhibit the respiratory activity at high ATP/ADP ratios, respectively. We propose that thermogenesis in mammals is related to subunit VIaL of cytochrome c oxidase with a H+/e(-) stoichiometry of 0.5 compared to 1.0 in the enzyme from bacteria or ectotherm animals. This hypothesis is supported by the lack of subunit VIa isoforms in cytochrome c oxidase from fish.
引用
收藏
页码：25 / 33
页数：9
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