Solvent isotope and viscosity effects on the steady-state kinetics of the flavoprotein nitroalkane oxidase

Giovanni Gadda, Paul F. Fitzpatrick

Research output: Contribution to journalArticle

10 Scopus citations


The flavoprotein nitroalkane oxidase catalyzes the oxidative denitrification of a broad range of primary and secondary nitroalkanes to yield the respective aldehydes or ketones, hydrogen peroxide and nitrite. With nitroethane as substrate the D2O(kcat/KM) value is 0.6 and the D2Okcat value is 2.4. The kcat proton inventory is consistent with a single exchangeable proton in flight, while the kcat/KM is consistent with either a single proton in flight in the transition state or a medium effect. Increasing the solvent viscosity did not affect the kcat or kcat/K M value significantly, establishing that nitroethane binding is at equilibrium and that product release does not limit kcat.

Original languageEnglish (US)
Pages (from-to)2785-2789
Number of pages5
JournalFEBS Letters
Issue number17
Publication statusPublished - Sep 2 2013



  • Flavoprotein
  • Michaelis-Menten kinetics
  • Nitroalkane oxidase
  • Solvent isotope effect
  • Viscosity

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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