1961
DOI: 10.1016/0006-3002(61)91077-0
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Diphosphopyridine nucleotide-linked nitrate reductase from Mycobacterium tuberculosis

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1963
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Cited by 5 publications
(2 citation statements)
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“…Nitrate reductase of M. tuberculosis is inhibited by tungstate, but this inhibition is reversed by molybdate. It is a particulate enzyme present constitutively in the organism (32). The enzyme is specific for NADH, and NADPH cannot replace NADH; 2,heptyl-4, hydroxyquinoline-N-oxide, a strong inhibitor of the oxidation of cytochrome b, inhibits the enzyme by 70% at a concentration of 1 um.…”
Section: Nitrogen Metabolismmentioning
confidence: 99%
“…Nitrate reductase of M. tuberculosis is inhibited by tungstate, but this inhibition is reversed by molybdate. It is a particulate enzyme present constitutively in the organism (32). The enzyme is specific for NADH, and NADPH cannot replace NADH; 2,heptyl-4, hydroxyquinoline-N-oxide, a strong inhibitor of the oxidation of cytochrome b, inhibits the enzyme by 70% at a concentration of 1 um.…”
Section: Nitrogen Metabolismmentioning
confidence: 99%
“…Although the presence of cytochromes in mycobacteria has been repeatedly demonstrated (Todd, 1949;Yamamura et al, 1955;Andrejew, Gernez-Rieux, and Tagguet, 1957;Bastarrachea and Goldman, 1961;Goldman et al, 1963), little is known of their variations.…”
mentioning
confidence: 99%