INVOLVEMENT OF INTRA-MITOCHONDRIAL PROTONS IN REDOX REACTIONS OF CYTOCHROME-A
INVOLVEMENT OF INTRA-MITOCHONDRIAL PROTONS IN REDOX REACTIONS OF CYTOCHROME-A
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DOI:
10.1016/0014-5793(78)80327-5
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发表时间:
1978-01-01
期刊:
影响因子:
3.5
通讯作者:
SKULACHEV, VP
中科院分区:
文献类型:
--
作者:
ARTZATBANOV, VY;KONSTANTINOV, AA;SKULACHEV, VP
The energy-conserving function of mitochondrial cytochrome oxidase has been widely believed to consist in the transmembrane transfer of an electron [l-4], as originally proposed by Mitchell [5]. On the other hand, involvement of protons in the cytochrome oxidase reaction was largely neglected (but see [6-8]), although reduction of oxygen to water needs not only 4 e-but also 4 H+ ions. We confirmed the important observation [9, 10] that Em of the high-potential heme of cytochrome oxidase was pH dependent [1 I]. We also found that it was pH inside mitochondria, that was ‘felt’by I?,,, of cytochrome oxidase [111. Since the high-potential component of cytochrome oxidase was thought at that time to represent heme a3 [2, 12-141, we interpreted our results as evidence for heme a3 being localized at the inner face of the mitochondrial membrane [111. Recent revision of the cytochrome oxidase spectral and potentiometric characteristics [15-171 made us re-investigate the problem. The data reported here (see also [181) indicate that:(1) Partial redox-linked protonation is characteristic of both cytochromes a and a3 in the high-potential redox transition of cytochrome oxidase.(2) Cytochrome a, known to react with cytochromeAbbreviations: E,, midpoint redox potential; CCCP, carbony1 cyanide mchlorophenyl hydrazone; Hepes, N-2-bydruxyetbylpiperazine-N-24hanesulfonate; Mops, morpholinopropanesulfonate; Tris, tris0lydroxymethYl) aminu methane