Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme

• Published in: Microbiology (Society for General Microbiology) Vol. 142; no. 2; pp. 251 - 260
• Main Authors: Higgins, Timothy P, Davey, Margaret, Trickett, Jim, Kelly, Don P, Murrell, J. Colin
• Format: Journal Article
• Language: English
• Published: Reading Soc General Microbiol 01.02.1996; Society for General Microbiology
• Subjects: Bacteria - metabolism; Bacteriology; Biodegradation, Environmental; Biological and medical sciences; Environmental Pollutants - metabolism; Flavin-Adenine Dinucleotide - metabolism; Fundamental and applied biological sciences. Psychology; Iron - metabolism; Mesylates - metabolism; Metabolism. Enzymes; Methanol - metabolism; Microbiology; Mutation; Oxygenases - antagonists & inhibitors; Oxygenases - isolation & purification; Oxygenases - metabolism; Substrate Specificity; Biodegradation; Oxygenase; Energy source; Enzymatic activity; Enzyme; Bacteria; Methanesulfonic acid; Metabolism; Methylotrophy
• ISSN: 1350-0872; 1465-2080
• DOI: 10.1099/13500872-142-2-251

1 Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK 2 Institute of Education, University of Warwick, Coventry CV4 7AL, UK ABSTRACT Summary: A novel methylotroph, strain M2, capable of utilizing methanesulfonic acid (MSA) as a sole source of carbon and energy was the subject of these investigations. The initial step in the biodegradative pathway of MSA in strain M2 involved an inducible NADH-specific monooxygenase enzyme (MSAMO). Partial purification of MSAMO from cell-free extracts by ion-exchange chromatography led to the loss of MSAMO activity. Activity was restored by the mixing of three distinct protein fractions designated A, B and C. The reconstituted enzyme had a narrow substrate specificity relative to crude cell-free extracts. Addition of FAD and ferrous ions to the reconstituted enzyme complex resulted in a fivefold increase in enzyme activity, suggesting the loss of FAD and ferrous ion from the multicomponent enzyme on purification. Analysis of mutants of strain M2 defective in the metabolism of C 1 compounds indicated that methanol was not an intermediate in the degradative pathway of MSA and also confirmed the involvement of a multicomponent enzyme in the degradation of MSA by methylotroph strain M2. Author for correspondence: J. Colin Murrell. Tel: +44 1203 52553. Fax: +44 1203 523568. e-mail: CM@dna.bio.warwick.ac.uk Keywords: methylotrophy, methanesulfonic acid (MSA), multicomponent enzyme, C 1 metabolism, alkyl sulfonates Deceased (12 April 1993).