Chemical and spectroscopic evidence for the formation of a ferryl Fea3 intermediate during turnover of cytochrome c oxidase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference20 articles.
1. Carbon monoxide-driven reduction of ferric heme and heme proteins.
2. The reduction of cytochrome c oxidase by carbon monoxide
3. The reactivity of pulsed cytochrome c oxidase toward carbon monoxide
4. Conformations of oxidized cytochrome c oxidase
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1. Oxygen Activation Mechanism at the Binuclear Site of Heme-Copper Oxidase Superfamily as Revealed by Time-Resolved Resonance Raman Spectroscopy;Progress in Inorganic Chemistry;2007-03-09
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3. Modulation of the Electron Redistribution in Mixed Valence Cytochrome c Oxidase by Protein Conformational Changes;Journal of Biological Chemistry;2004-03
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