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- W2000225774 abstract "The oxidation-reduction potentials (E1 and E2) of azotoflavin determined by equilibration with indicator dyes were −464 and −270 mV, respectively, at pH 7.7. The reduction of azotoflavin to the semiquinone was greatly stimulated by catalytic concentrations of methyl viologen and was observed with three diverse reducing systems: dithionite, illuminated chloroplasts, and NADPH plus ferredoxin-NADP reductase. The rate of semiquinone oxidation was increased 10- to 15-fold by methyl viologen at 6.25 × 10−6 M. Biological activity of azotoflavin in the nitrogenase reaction was considerably stimulated by addition of low concentrations of azotobacter ferredoxin or methyl viologen. The joint requirement for azotoflavin and ferredoxin for maximal nitrogenase activity is discussed in reference to recent suggestions on renaming azotoflavin." @default.
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- W2000225774 date "1972-10-01" @default.
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- W2000225774 title "The electron transport system in nitrogen fixation by azotobacter. IV. Some oxidation-reduction properties of azotoflavin" @default.
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- W2000225774 doi "https://doi.org/10.1016/0006-291x(72)90415-9" @default.
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