Nitroalkane oxidase, a carbanion-forming flavoprotein homologous to acyl-CoA dehydrogenase

Paul F. Fitzpatrick, Allen M. Orville, Akanksha Nagpal, Michael P. Valley

Research output: Contribution to journalArticlepeer-review

45 Scopus citations

Abstract

While several flavoproteins will oxidize nitroalkanes in addition to their physiological substrates, nitroalkane oxidase (NAO) is the only one which does not require the anionic nitroalkane. This, in addition to the induction of NAO by nitroethane seen in Fusarium oxysporum, suggests that oxidation of a nitroaliphatic species is the physiological role of the enzyme. Mechanistic studies of the reaction with nitroethane as substrate have established many of the details of the enzymatic reaction. The enzyme is unique in being the only flavoprotein to date for which a carbanion is definitively established as an intermediate in catalysis. Recent structural analyses show that NAO is homologous to the acyl-CoA dehydrogenase and acyl-CoA oxidase families of enzymes. In NAO, the glutamate which acts as the active site base in the latter enzymes is replaced by an aspartate.

Original languageEnglish (US)
Pages (from-to)157-165
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume433
Issue number1
DOIs
StatePublished - Jan 1 2005

Keywords

  • Acyl-CoA dehydrogenase
  • Acyl-CoA oxidase
  • Flavoprotein
  • Mechanism
  • Nitroalkane oxidase
  • Structure

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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