Molecular structure of a heme-copper redox center of the Escherichia coli ubiquinol oxidase: evidence and model.
Biochemical, spectroscopic, and molecular biological studies on bacterial respiratory oxidases in the last decade have greatly increased our understanding of a molecular structure of the metal centers which catalyze the dioxygen reduction chemistry. Based upon the latest physicochemical and molecular biological evidence and theoretical consideration of a folding mechanics of membrane proteins, we propose here the tertiary structure of the heme-copper metal center of the Escherichia coli bo-type ubiquinol oxidase, the cytochrome bo complex. The molecular mechanism of electron transfer-coupled proton pumping in the heme-copper respiratory oxidases is reviewed on the basis of this predicted model.
Department of Plant Sciences, Graduate School of Science, University of Tokyo.
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Mogi
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Nakamura
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Anraku
D000595:Amino Acid Sequence; D003300:Copper / Q000737:chemistry*; D003573:Cytochrome b Group; D003580:Cytochromes / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D006418:Heme / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010084:Oxidation-Reduction; D013329:Structure-Activity Relationship
D003573:Cytochrome b Group; D003580:Cytochromes; D029968:Escherichia coli Proteins; D006418:Heme; D003300:Copper; C017168:cytochrome bo, E coli