NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase

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NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase.

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 ...

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Ubiquinol oxidase has been reconstituted from ubiquinol-cytochrome c reductase (Complex III), cytochrome c and cytochrome c oxidase (Complex IV). The steady-state level of reduction of cytochrome c by ubiquinol-2 varies with the molar ratios of the complexes and with the presence of antimycin in a way that can be quantitatively accounted for by a model in which cytochrome c acts as a freely dif...

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Proton 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...

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Dynamics of electron transfer pathways in cytochrome C oxidase.

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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Proton pumping in cytochrome c oxidase: the coupling between proton and electron gating.

C ytochrome c oxidase is the terminal oxidase in cellular respiration. This membrane protein accepts electrons from ferrocytochrome c in the periplasmic space of the mitochondrion, one electron at a time, and transfers the reducing equivalents to the binuclear heme-iron copper site (the socalled Fea3, CuB site), where dioxygen binds and the O·O bond is subsequently cleaved (1). In this manner, ...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 2011

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.1108320108