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Nitrite Mode of Action: Inhibition of Yeast Pyruvate Decarboxylase (E.C. 4.1.1.1) and Clostridial Pyruvate:Ferredoxin Oxidoreductase (E.C. 1.2.7.1) by Nitric Oxide
Author(s) -
McMINDES M.K.,
SIEDLER A.J.
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb08985.x
Subject(s) - chemistry , pyruvate decarboxylation , nitrite , decarboxylation , biochemistry , sodium nitrite , dihydrolipoyl transacetylase , sodium pyruvate , nitric oxide , pyruvate decarboxylase , pyruvate dehydrogenase complex , enzyme , food science , organic chemistry , catalysis , nitrate , alcohol dehydrogenase
The effects of nitric oxide (NO) on the nonoxidative decarboxylation of pyruvate were studied using yeast pyruvate decarboxylase (PD) as a model. PD was inhibited by NO (50% inhibition 0.5 mM) under anaerobic but not under aerobic conditions. Prior inhibition by NO was not reversed by aerobic conditions. Sodium nitrite (0.5 mM) was not inhibitory. Inhibition of PD by NO was markedly enhanced in the presence of ascorbate. A preparation of pyruvate:ferredoxin oxidoreductase (PFO) from Clostridium perfringens (3624 A) was inhibited by NO (50% inhibition 0.025 mM) but not by sodium nitrite (1.0 mM). These results suggest that the thiamin dependent decarboxylation of pyruvate may be an additional site for the antimicrobial mode of action of nitrite independent of the iron‐sulfur center of PFO and supports the concept that the active principle is NO.