Metabolic role of flavoprotein in terminal oxidation by cytochrome o from Vitreoscilla

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NADH-cytochrome o reductase is associated with purified preparations of cytochrome o and these preparations can be separated into "reductase enriched" and "reductase-poor" fractions by column chromatography. Direct evidence for the presence of flavin in these preparations was obtained from fluorescence spectra, and the intensity of the fluorescence maxima was greater in reductase-enriched preparations of cytochrome o than in reductase-poor ones. Exogenously added flavin stimulated the rate of NADH oxidation by molecular oxygen that is catalyzed by preparations of cytochrome o, more stimulation being observed with "reductase-poor" than with "reductase-enriched" preparations. Since reduction of cytochrome o in an aerobic solution was also stimulated by added flavin, the primary effect of the latter is on the NADH-cytochrome o reductase side of the cytochrome. Possible explanations for the observed stimulation of the reduction of cytochrome o in aerobic solutions in the presence of exogenous flavin are 1) reconstitution of flavin-deficient reductase, 2) flavin acting as a mobile electron carrier between the reductase and the cytochrome, 3) cytochrome o being reduced by superoxide anion generated as an intermediate in the reaction of reduced flavin with oxygen. More direct evidence for the participation of a flavoprotein in the reduction of cytochrome o was the observed photochemical reduction of cytochrome o in an anaerobic CO atmosphere without added flavin using EDTA as an electron donor.
日本植物生理学会の論文

Metabolic role of flavoprotein in terminal oxidation by cytochrome o from Vitreoscilla

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