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- W2002201426 abstract "1. Nitrate reductase from the bacterium, Achromobacter fischeri, has been highly purified and separated from other electron-transport systems. The color and the spectrum of the reduced enzyme preparation indicate the presence of a cytochrome with absorption peaks at 550, 520, and 419 mμ. 2. The enzyme catalyzes the reduction of nitrate with reduced benzylviologen as an electron donor. DPNH will serve as an electron donor only when a bacterial DPNH-cytochrome reductase system is added. 3. The reduction of nitrate by benzylviologen is not affected by carbon monoxide, cyanide, o-phenanthroline, and other metal-chelating agents. The enzyme is, however, inhibited by p-chloromercuribenzoate; this inhibition is reversed by various —SH containing compounds. 4. The reduction of nitrate by DPNH is affected by all of the inhibitors mentioned above. Of particular importance is the observation that a pink color appears when o-phenanthroline and α,α-dipyridyl are used. The results suggest a catalytic role for inorganic iron. Flavine is required in this system. Reduced FMN can also function as an electron donor. 5. Carbon monoxide inhibition of nitrate reduction by DPNH and the reversal by light suggests the involvement of a specific cytochrome. Spectral evidence indicates a reduction of the bacterial cytochrome by the reductase and its reoxidation by nitrate. 6. The effect of enzyme, nitrate, and flavine concentration as well as pH, temperature, electron donors, and various inhibitors on nitrate reduction have been studied." @default.
- W2002201426 created "2016-06-24" @default.
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- W2002201426 creator A5062550652 @default.
- W2002201426 date "1957-03-01" @default.
- W2002201426 modified "2023-10-10" @default.
- W2002201426 title "Nitrate reductase from Achromobacter fischeri. Purification and properties: Function of flavines and cytochrome" @default.
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- W2002201426 doi "https://doi.org/10.1016/0003-9861(57)90242-4" @default.
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