Mechanism for sulfur acquisition by the alkanesulfonate monooxygenase system

Bioorg Chem. 2011 Dec;39(5-6):178-84. doi: 10.1016/j.bioorg.2011.08.001. Epub 2011 Aug 10.

Abstract

The bacterial alkanesulfonate monooxygenase system is involved in the acquisition of sulfur from organosulfonated compounds during limiting sulfur conditions. The reaction relies on an FMN reductase to supply reduced flavin to the monooxygenase enzyme. The reaction catalyzed by the alkanesulfonate monooxygenase enzyme involves the carbon-sulfur bond cleavage of a wide range of organosulfonated compounds. A C4a-(hydro)peroxyflavin is the oxygenating intermediate in the mechanism of desulfonation by the alkanesulfonate monooxygenase. This review discusses the physiological importance of this system, and the individual kinetic parameters and mechanistic properties of this enzyme system.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Alkanesulfonates / metabolism*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / metabolism
  • FMN Reductase / chemistry
  • FMN Reductase / metabolism
  • Mixed Function Oxygenases / chemistry*
  • Mixed Function Oxygenases / metabolism*
  • Protein Conformation

Substances

  • Alkanesulfonates
  • Escherichia coli Proteins
  • Mixed Function Oxygenases
  • SsuD protein, E coli
  • FMN Reductase
  • SsuE protein, E coli