title: Mechanism for sulfur acquisition by the alkanesulfonate monooxygenase system.
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.
authors: The Department of Chemistry and Biochemistry, Auburn University, AL 36849, United States. ellishr@auburn.edu
authors: Holly R
authors: HR
authors: Ellis
mesh_terms: D000476:Alkanesulfonates / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D038181:FMN Reductase / Q000737:chemistry / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation
chemical_list: D000476:Alkanesulfonates; D029968:Escherichia coli Proteins; D006899:Mixed Function Oxygenases; C499579:SsuD protein, E coli; D038181:FMN Reductase; C447459:SsuE protein, E coli