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- W1863137816 abstract "Kemp, John D. (University of California, Los Angeles), and Daniel E. Atkinson . Nitrite reductase of Escherichia coli specific for reduced nicotinamide adenine dinucleotide. J. Bacteriol. 92: 628–634. 1966.—A nitrite reductase specific for reduced nicotinamide adenine dinucleotide (NADH 2 ) appears to be responsible for in vivo nitrite reduction by Escherichia coli strain Bn. In extracts, the reduction product is ammonium, and the ratio of NADH 2 oxidized to nitrite reduced or to ammonium produced is 3. The Michaelis constant for nitrite is 10 μ m . The enzyme is induced by nitrite, and the ability of intact cells to reduce nitrite parallels the level of NADH 2 -specific nitrite reductase activity demonstrable in cell-free preparations. Crude extracts of strain Bn will also reduce hydroxylamine, but not nitrate or sulfite, at the expense of NADH 2 . Kinetic observations indicate that hydroxylamine and nitrite may both be reduced at the same active site. The high apparent Michaelis constant for hydroxylamine (1.5 m m ), however, seems to exclude hydroxylamine as an intermediate in nitrite reduction. In vitro activity is enhanced by preincubation with nitrite, and decreased by preincubation with NADH 2 ." @default.
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- W1863137816 date "1966-09-01" @default.
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- W1863137816 title "Nitrite Reductase of Escherichia coli Specific for Reduced Nicotinamide Adenine Dinucleotide" @default.
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- W1863137816 doi "https://doi.org/10.1128/jb.92.3.628-634.1966" @default.
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