Kinetic analysis of substrate inhibition in nitric oxide reductase of Paracoccus denitrificans
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
10462514
DOI
10.1006/bbrc.1999.1245
PII: S0006-291X(99)91245-7
Knihovny.cz E-zdroje
- MeSH
- chemické modely MeSH
- kinetika MeSH
- oxid dusnatý metabolismus farmakologie MeSH
- oxidoreduktasy antagonisté a inhibitory metabolismus MeSH
- Paracoccus denitrificans enzymologie MeSH
- tetramethylfenylendiamin metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- nitric-oxide reductase MeSH Prohlížeč
- oxid dusnatý MeSH
- oxidoreduktasy MeSH
- tetramethylfenylendiamin 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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