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• W2072579418 abstract "The nitrite reductase from A. fischeri has been purified 83-fold and obtained in an ultracentrifugally and electrophoretically homogeneous form. The enzyme has been characterized as a heme c-containing protein. The molecular weight of the enzyme is 95,000 ± 4,000. Two moles of heme c are present per mole of the enzyme. The reduced enzyme is autooxidizable. The purified enzyme reduces nitrite and hydroxylamine stoichiometrically to ammonia. The ratio of NADH oxidized to nitrite reduced is 3, and that of reduced benzyl viologen oxidized to nitrite reduced is 6. The respective values for hydroxylamine reduction are 1 and 2, respectively. The Km for nitrite is 0.05 mm and for hydroxylamine 5–8 mm. The enzyme will not reduce nitrate or sulfite. The high Km for hydroxylamine however seems to exclude hydroxylamine as a free intermediate in nitrite reduction. The effect of enzyme, nitrite and flavin concentrations as well as pH, temperature, electron donors and various inhibitors on nitrite reduction has been studied. The bacterial NAD(P)H-flavin reductase is not inhibited by respiratory chain inhibitors or metal-binding agents except o-phenanthroline and α,α′-dipyridyl. CO, cyanide and sulfhydryl agents also do not inhibit NAD(P)H-flavin reductase." @default.
• W2072579418 created "2016-06-24" @default.
• W2072579418 creator A5048937098 @default.
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• W2072579418 date "1972-02-01" @default.
• W2072579418 modified "2023-09-27" @default.
• W2072579418 title "Purification, characterization and properties of nitrite reductase of Achromobacter fischeri" @default.
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• W2072579418 doi "https://doi.org/10.1016/0003-9861(72)90181-6" @default.
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