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Formation of a potent respiratory inhibitor at nitrite reduction by nitrite reductase isolated from the bacterium Paracoccus denitrificans
Author(s) -
Kučera Igor,
Skládal Petr
Publication year - 1990
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620300712
Subject(s) - paracoccus denitrificans , periplasmic space , nitrite reductase , nitrite , chemistry , biochemistry , reductase , oxidase test , respiratory chain , enzyme , cytochrome c oxidase , cytochrome c , chromatography , nitrate reductase , organic chemistry , nitrate , escherichia coli , mitochondrion , gene
A new method of dissimilatory nitrite reductase (cytochrome cd 1 ) isolation from the periplasmic fraction of anaerobically grown cells of the bacterium Paracoccus denitrificans was developed, using ionex and gel permeation chromatography with FPLC system (PHARMACIA, Sweden). In experiments with isolated enzyme it was shown that through a nitrite reduction, catalysed by this enzyme, a substance (presumably nitric oxide) was formed which at submicromolar concentrations inhibited terminal cytochrome oxidase of the respiratory chain of the same bacterium. These results help to explain formerly observed sensitivity of bacterial oxidase activity to NO ‐ 2 and the mechanism of switching the electron flow from O 2 to nitrogen terminal acceptors.