reply: Proton pumping by cytochrome c oxidase

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Proton pumping by cytochrome c oxidase.

Proton Pumping in Cotychrome c Oxidase by Jianxun Lu Advisor: Professor Marilyn Gunner Cytochrome c oxidase (CcO) is a large trans-membrane protein, which is the final enzyme in the respiratory electron transport chain in mitochondria or aerobic bacteria. It implements proton pumping through the mitochondrial membrane against the electrochemical gradient, by utilizing the chemical energy releas...

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Proton-pumping mechanism of cytochrome C oxidase.

Cytochrome c oxidase (CcO), as the terminal oxidase of cellular respiration, coupled with a proton-pumping process, reduces molecular oxygen (O(2)) to water. This intriguing and highly organized chemical process represents one of the most critical aspects of cellular respiration. It employs transition metals (Fe and Cu) at the O(2) reduction site and has been considered one of the most challeng...

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The mechanism of proton pumping by cytochrome c oxidase

Cytochrome c oxidase catalyzes the reduction of oxygen to water that is accompanied by pumping of four protons across the mitochondrial or bacterial membrane. Triggered by the results of recent x-ray crystallographic analyses, published data concerning the coupling of individual electron transfer steps to proton pumping are reanalyzed: Conversion of the conventional oxoferryl intermediate F to ...

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Kinetics of proton pumping in cytochrome c oxidase.

We propose a simple model of cytochrome c oxidase, including four redox centers and four protonable sites, to study the time evolution of electrostatically coupled electron and proton transfers initiated by the injection of a single electron into the enzyme. We derive a system of master equations for electron and proton state probabilities and show that an efficient pumping of protons across th...

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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: Nature

سال: 1999

ISSN: 0028-0836,1476-4687

DOI: 10.1038/45135