Boden, Rich, Borodina, E., Wood, A. P., Kelly, D. P., Murrell, J. C. (J. Colin) and Schäfer, Hendrik. (2011) Purification and characterization of dimethylsulfide monooxygenase from hyphomicrobium sulfonivorans. Journal of Bacteriology, Vol.193 (No.5). pp. 1250-1258. ISSN 0021-9193

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Abstract

Dimethylsulfide (DMS) is a volatile organosulfur compound which has been implicated in the biogeochemical cycling of sulfur and in climate control. Microbial degradation is a major sink for DMS. DMS metabolism in some bacteria involves its oxidation by a DMS monooxygenase in the first step of the degradation pathway; however, this enzyme has remained uncharacterized until now. We have purified a DMS monooxygenase from Hyphomicrobium sulfonivorans, which was previously isolated from garden soil. The enzyme is a member of the flavin-linked monooxygenases of the luciferase family and is most closely related to nitrilotriacetate monooxygenases. It consists of two subunits: DmoA, a 53-kDa FMNH(2)-dependent monooxygenase, and DmoB, a 19-kDa NAD(P) H-dependent flavin oxidoreductase. Enzyme kinetics were investigated with a range of substrates and inhibitors. The enzyme had a K(m) of 17.2 (+/- 0.48) mu M for DMS (k(cat) = 5.45 s(-1)) and a V(max) of 1.25 (+/- 0.01) mu mol NADH oxidized min(-1) (mg protein -1). It was inhibited by umbelliferone, 8-anilinonaphthalenesulfonate, a range of metal-chelating agents, and Hg(2+), Cd(2+), and Pb(2+) ions. The purified enzyme had no activity with the substrates of related enzymes, including alkanesulfonates, aldehydes, nitrilotriacetate, or dibenzothiophene-sulfone. The gene encoding the 53-kDa enzyme subunit has been cloned and matched to the enzyme subunit by mass spectrometry. DMS monooxygenase represents a new class of FMNH(2)-dependent monooxygenases, based on its specificity for dimethylsulfide and the molecular phylogeny of its predicted amino acid sequence. The gene encoding the large subunit of DMS monooxygenase is colocated with genes encoding putative flavin reductases, homologues of enzymes of inorganic and organic sulfur compound metabolism, and enzymes involved in riboflavin synthesis.

Item Type:	Journal Article
Subjects:	Q Science > QP Physiology Q Science > QR Microbiology
Divisions:	Faculty of Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH):	Dimethyl sulfide, Monooxygenases, Microbial metabolism, Biogeochemistry
Journal or Publication Title:	Journal of Bacteriology
Publisher:	American Society for Microbiology
ISSN:	0021-9193
Date:	March 2011
Volume:	Vol.193
Number:	No.5
Page Range:	pp. 1250-1258
Identification Number:	10.1128/JB.00977-10
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Funder:	Natural Environment Research Council (Great Britain) (NERC)
URI:	http://wrap.warwick.ac.uk/id/eprint/36662

Data sourced from Thomson Reuters' Web of Knowledge

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