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efficient, N-terminally truncated protein
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0.2 mM quinone stimulates reaction with D-alanine and oxidized 2,6-dichloroindophenol 2fold
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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
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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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