Kinetic analysis of substrate inhibition in nitric oxide reductase of Paracoccus denitrificans
Language English Country United States Media print
Document type Journal Article
PubMed
10462514
DOI
10.1006/bbrc.1999.1245
PII: S0006-291X(99)91245-7
Knihovny.cz E-resources
- MeSH
- Models, Chemical MeSH
- Kinetics MeSH
- Nitric Oxide metabolism pharmacology MeSH
- Oxidoreductases antagonists & inhibitors metabolism MeSH
- Paracoccus denitrificans enzymology MeSH
- Tetramethylphenylenediamine metabolism MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- nitric-oxide reductase MeSH Browser
- Nitric Oxide MeSH
- Oxidoreductases MeSH
- Tetramethylphenylenediamine MeSH
The current kinetic model for the nitric oxide reductase reaction (Girsch, P., and de Vries, S. (1997) Biochim. Biophys. Acta 1318, 202-216) does not involve the concentration of an electron donor. Here we introduce this variable and show, both theoretically and experimentally, its role in determining the extent of substrate inhibition by the excess of nitric oxide. NO is found to inhibit competitively with the electron donor, possibly by binding to the oxidized form of the enzyme. The observed partial character of the inhibition is tentatively explained by a slow reduction of the non-productive NO complex.
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