Improved X-ray structures of bovine heart cytochrome c oxidase reveal redox-driven proton active transports by Mg2+-containing water cluster
نویسندگان
چکیده
[1] B. Kadenbach, R. Ramzan, L. Wen, S. Vogt, New extension of the Mitchell Theory for oxidative phosphorylation in mitochondria of living organisms, Biochim. Biophys. Acta. 1800 (2010) 205–12. [2] R. Ramzan, K. Staniek, B. Kadenbach, S. Vogt, Mitochondrial respiration and membrane potential are regulated by the allosteric ATP-inhibition of cytochrome c oxidase, Biochim. Biophys. Acta. 1797 (2010) 1672–80.
منابع مشابه
Cytochrome c oxidase.
Within the past year, the structures of the cytochrome c oxidase from the soil bacterium Paracoccus denitrificans and of the metal centers of the cytochrome c oxidase from bovine heart mitochondria, both determined at 2.8 A resolution by X-ray crystallography, have been reported. The structures form a basis for understanding the mechanism of this redox-coupled transmembrane proton pump, which i...
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Bovine heart cytochrome c oxidase is a large multi-component membrane protein containing several phospholipids. X-ray structures of this enzyme at high resolution, determined recently, show a trigonal planar structure of CuB site in the O2 reduction site, which could contribute critically to the four-electron reduction of O2 bound at haem a3, and a hydrogen bond network, through which the proto...
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Mitochondrial cytochrome c oxidase plays an essential role in aerobic cellular respiration, reducing dioxygen to water in a process coupled with the pumping of protons across the mitochondrial inner membrane. An aspartate residue, Asp-51, located near the enzyme surface, undergoes a redox-coupled x-ray structural change, which is suggestive of a role for this residue in redox-driven proton pump...
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Cytochrome c oxidase is a redox-driven proton pump, which couples the reduction of oxygen to water to the translocation of protons across the membrane. The recently solved x-ray structures of cytochrome c oxidase permit molecular dynamics simulations of the underlying transport processes. To eventually establish the proton pump mechanism, we investigate the transport of the substrates, oxygen a...
متن کاملX-ray structure and reaction mechanism of bovine heart cytochrome c oxidase.
X-ray structure of bovine heart cytochrome c oxidase in the fully oxidized state shows a peroxide bridging between Fe2+ and Cu2+ in the O2 reduction site. The bond distances for Fe-O and Cu-O are 2.52 and 2.16 A, respectively. The structure is consistent with antiferromagnetic coupling between the two metals, which has long been known and to recent redox titration results [J. Biol. Chem. 274 (1...
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تاریخ انتشار 2014