Chen, Yin, Patel, Nisha A., Crombie, Andrew, Scrivens, James H. and Murrell, J. C. (J. Colin) (2011) Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase. Proceedings of the National Academy of Sciences, Vol.108 (No.43). pp. 17791-17796. doi:10.1073/pnas.1112928108 ISSN 0027-8424.

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Abstract

Flavin-containing monooxygenases (FMOs) are one of the most important monooxygenase
systems in Eukaryotes and have many important physiological functions. FMOs have also
been found in bacteria; however, their physiological function is not known. Here, we report
the identification and characterization of trimethylamine (TMA) monooxygenase, termed
tmm, from Methylocella silvestris, using a combination of proteomic, biochemical and
genetic approaches. This bacterial FMO contains the FMO sequence motif
(FXGXXXHXXXF/Y) and typical flavin adenine dinucleotide and nicotinamide adenine
dinucleotide phosphate-binding domains. The enzyme was highly expressed in TMA-grown
M. silvestris and absent during growth on methanol. The gene, tmm, was expressed in
Escherichia coli and the purified recombinant protein had high TMA monooxygenase
activity. Mutagenesis of this gene abolished the ability of M. silvestris to grow on TMA as a
sole carbon and energy source. Close homologs of tmm occur in many Alphaproteobacteria,
in particular Rhodobacteraceae (marine “Roseobacter” clade, MRC) and the marine SAR11
clade (Pelagibacter ubique). We showed that the ability for MRC to use TMA as sole carbon
and/or nitrogen source is directly linked to the presence of tmm in their genomes and purified
Tmm of MRC and SAR11 from recombinant E. coli showed TMA monooxygenase activities.
The tmm gene is very abundant in the metagenomes of the Global Ocean Sampling
Expedition and we estimate that 20% of the bacteria in the surface ocean contain tmm. Taken
together, our results suggest that TMA monooxygenase, a bacterial FMO, plays an important,
yet overlooked, role in the global carbon and nitrogen cycles.

Item Type:	Journal Article
Subjects:	Q Science > QR Microbiology
Divisions:	Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH):	Monooxygenases -- Physiological effect, Methanotrophs -- Physiology
Journal or Publication Title:	Proceedings of the National Academy of Sciences
Publisher:	National Academy of Sciences
ISSN:	0027-8424
Official Date:	25 October 2011
Dates:	Date Event 25 October 2011 UNSPECIFIED
Volume:	Vol.108
Number:	No.43
Page Range:	pp. 17791-17796
DOI:	10.1073/pnas.1112928108
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Date of first compliant deposit:	18 December 2015
Date of first compliant Open Access:	18 December 2015
Funder:	Natural Environment Research Council (Great Britain) (NERC)
Grant number:	NE/H016236/1 (NERC), NE/E016855/1 (NERC)

Data sourced from Thomson Reuters' Web of Knowledge

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