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efficient, N-terminally truncated protein
-
0.2 mM quinone stimulates reaction with D-alanine and oxidized 2,6-dichloroindophenol 2fold
-
the bound ubiquinone at the QH site of cytochrome bo is essential for the catalytic turnover of the oxidase reactions, but it is not necessary for re-reduction of ferric heme b after the heme b-to-heme o electron transfer under flow-flash conditions
the bound ubiquinone at the QH site of cytochrome bo is essential for the catalytic turnover of the oxidase reactions, but it is not necessary for re-reduction of ferric heme b after the heme b-to-heme o electron transfer under flow-flash conditions
the bound ubiquinone at the QH site of cytochrome bo is essential for the catalytic turnover of the oxidase reactions, but it is not necessary for re-reduction of ferric heme b after the heme b-to-heme o electron transfer under flow-flash conditions
the bound ubiquinone at the QH site of cytochrome bo is essential for the catalytic turnover of the oxidase reactions, but it is not necessary for re-reduction of ferric heme b after the heme b-to-heme o electron transfer under flow-flash conditions
the enzyme contains one equivalent of ubiquinone-8
the enzyme contains one equivalent of ubiquinone-8
the enzyme contains one equivalent of ubiquinone-8
the enzyme contains one equivalent of ubiquinone-8
complex contains one non-covalently bound FAD, one noncovalently bound riboflavin, ubiquinone-8 and a [2Fe2S] cluster
-
the enzyme contains one ubiquinone-8
-
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Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B
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Reconstitution of the Ubiquinone-dependent pyruvate oxidase system of Escherichia coli with the cytochrome o terminal oxidase complex
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Crystallization of the Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae
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Quinone reduction by the Na+-translocating NADH dehydrogenase promotes extracellular superoxide production in Vibrio cholerae
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The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli
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Role of a bound ubiquinone on reactions of the Escherichia coli cytochrome bo with ubiquinol and dioxygen
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Localization and function of the membrane-bound riboflavin in the Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) from Vibrio cholerae
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The single NqrB and NqrC subunits in the Na(+)-translocating NADH: quinone oxidoreductase (Na(+)-NQR) from Vibrio cholerae each carry one covalently attached FMN
2012
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Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB
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2008
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