The possible role of isoforms of cytochrome c oxidase subunit VIa in mammalian thermogenesis

被引：18
|
作者：
Hüttemann, M [1 ]
Frank, V [1 ]
Kadenbach, B [1 ]
机构：
[1] Univ Marburg, Fachbereich Chem, D-35032 Marburg, Germany
来源：
CELLULAR AND MOLECULAR LIFE SCIENCES | 1999年 / 55卷 / 11期
关键词：
cytochrome c oxidase; H+/e(-) stoichiometry; evolution; mammalian thermogenesis; fish tissues; homeothermy; efficiency of energy transduction;
D O I：
10.1007/s000180050387
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：
A single cDNA of cytochrome c oxidase subunit Via was characterised from liver, heart and the thermogenic organ of the partially endotherm tuna fish. The amino acid sequence revealed high identity with subunit VIa from carp and trout. but low identity to subunits VIaL (liver type) and VIaH (heart type) of mammalian cytochrome c oxidase. In reconstituted cytochrome c oxidase from bovine heart, the H+/e(-) stoichiometry is decreased from 1.0 to 0.5 at high intraliposomal ATP/ADP ratios via exchange of bound ADP by ATP at the matrix domain of the transmembraneous subunit VIaH. Reconstituted cytochrome c oxidase from bovine liver and kidney, containing subunit VIaL, revealed H+/e(-) ratios below 0.5, independent of the ATP/ADP ratio. The results suggest the evolution of three types of subunit VIa. Subunits VIaH and VIaL are postulated to participate in mammalian thermogenesis.
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收藏
页码：1482 / 1490
页数：9
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