Purification and Some Properties of Nitrite Reductase from Clostridium perfringens

Nitrite reductase from Clostridium perfringens was purified by chromatographies on DEAE-cellulose, DEAE-Sephadex, Sephadex G-150, and hydroxylapatite and by isoelectric focussing to a homogeneous state, showing essentially a single protein band in disc gel electrophoresis and a single immuno-precipi...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1983-01, Vol.94 (4), p.1053-1059
Main Authors: SEKIGUCHI, Satoshi, SEKI, Sachiko, ISHIMOTO, Makoto
Format: Article
Language:English
Subjects:
Clostridium perfringens
Clostridium perfringens - enzymology
Electron Transport
Immunodiffusion
Kinetics
Molecular Weight
NADH, NADPH Oxidoreductases - isolation & purification
nitrite reductase
Nitrite Reductases - isolation & purification
Nitrite Reductases - metabolism
Species Specificity
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Summary:Nitrite reductase from Clostridium perfringens was purified by chromatographies on DEAE-cellulose, DEAE-Sephadex, Sephadex G-150, and hydroxylapatite and by isoelectric focussing to a homogeneous state, showing essentially a single protein band in disc gel electrophoresis and a single immuno-precipitation line in double diffusion against antiserum obtained from immunized rabbits. The reductase was induced in the presence of nitrate. It had a molecular weight of 54,000 and showed no absorption peak in the visible region. The pH optimum was 6.2 and Km for nitrite was 5 mM. Ferredoxin, as well as viologen dyes, was found to be an electron donor. The product of nitrite reduction was hydroxylamine. This reductase was inhibited by o-phenanthroline and azide but not by cyanide or diethyldithiocarbamate.
ISSN:0021-924X
DOI:10.1093/oxfordjournals.jbchem.a134447