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Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Alcaligenes faecalis strain S-6.

Authors
  • Kakutani, T
  • Watanabe, H
  • Arima, K
  • Beppu, T
Type
Published Article
Journal
Journal of biochemistry
Publication Date
Feb 01, 1981
Volume
89
Issue
2
Pages
453–461
Identifiers
PMID: 7240122
Source
Medline
License
Unknown

Abstract

A copper-containing nitrite reductase was purified and crystallized from a potent denitrifying bacterium, Alcaligenes faecalis strain S-6. The enzyme was composed of 4 subunits with a molecular weight of about 30,000, each containing 1 atom of Cu2+. Nitric oxide was identified as a main reduction product from nitrite in the enzyme-catalyzed reaction. The enzyme activity was inhibited strongly by KCN but only slightly by sulfhydryl reagents such as p-chloromercuribenzoate and N-ethylmaleimide.

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