Crystallization of part of the mitochondrial electron transfer chain: cytochrome c oxidase--cytochrome c complex.
نویسندگان
چکیده
منابع مشابه
The Cytochrome C-cytochrome Oxidase Complex
In the preceding paper the oxidation of substrates by “indophenol oxidase” was demonstrated to be a joint action of cytochrome and cytochrome oxidase. It was further shown that with a given amount of oxidase the velocity of hydroquinone oxidation reached a maximum as the amount of added cytochrome was increased. The latter fact immediately suggested the probability that the rapid aerobic oxidat...
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Cytochrome c oxidase mediates the final step of electron transfer reactions in the respiratory chain, catalyzing the transfer between cytochrome c and the molecular oxygen and concomitantly pumping protons across the inner mitochondrial membrane. We investigate the electron transfer reactions in cytochrome c oxidase, particularly the control of the effective electronic coupling by the nuclear t...
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The final interprotein electron transfer (ET) in the mammalian respiratory chain, from cytochrome c (Cyt c) to cytochrome c oxidase (CcO) is investigated by (1)H-(15)N heteronuclear single quantum coherence spectral analysis. The chemical shift perturbation in isotope-labeled Cyt c induced by addition of unlabeled CcO indicates that the hydrophobic heme periphery and adjacent hydrophobic amino ...
متن کاملProton uptake controls electron transfer in cytochrome c oxidase.
In cytochrome c oxidase, a requirement for proton pumping is a tight coupling between electron and proton transfer, which could be accomplished if internal electron-transfer rates were controlled by uptake of protons. During reaction of the fully reduced enzyme with oxygen, concomitant with the "peroxy" to "oxoferryl" transition, internal transfer of the fourth electron from CuA to heme a has t...
متن کاملCytochrome c oxidase: decay of the primary oxygen intermediate involves direct electron transfer from cytochrome a.
The decay of the primary intermediate generated in the reaction of oxygen with cytochrome c oxidase is nearly one order of magnitude faster in the fully reduced form of the enzyme than it is in the mixed valence form. To account for this observation, we propose a model describing the early molecular events in the reaction. In this model the decay of the primary Fe-O2 intermediate in the fully r...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1980
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.77.2.928