Boden, Rich and Murrell, J. C. (J. Colin). (2011) Response to mercury (II) ions in Methylococcus capsulatus (Bath). FEMS Microbiology Letters, Vol.324 (No.2). pp. 106-110. ISSN 0378-1097

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Abstract

The mercury (II) ion is toxic and is usually detoxified in Bacteria by reduction to elemental mercury, which is less toxic. This is catalysed by an NAD(P)H-dependent mercuric reductase (EC 1.16.1.1). Here, we present strong evidence that Methylococcus capsulatus (Bath) - a methanotrophic member of the Gammaproteobacteria - uses this enzyme to detoxify mercury. In radiorespirometry studies, it was found that cells exposed to mercury dissimilated 100% of [(14)C]methane provided to generate reducing equivalents to fuel mercury (II) reduction, rather than the mix of assimilation and dissimilation found in control incubations. The detoxification system is constitutively expressed with a specific activity of 352 (+/- 18) nmol NADH oxidized min(-1) (mg protein)(-1). Putative mercuric reductase genes were predicted in the M. capsulatus (Bath) genome and found in mRNA microarray studies. The MerA-derived polypeptide showed high identity (> 80%) with MerA sequences from the Betaproteobacteria.

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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):	Heavy metals -- Physiological effect, Flavoproteins, Methanotrophs, Oxidoreductases, Metal ions -- Metabolism
Journal or Publication Title:	FEMS Microbiology Letters
Publisher:	Wiley-Blackwell Publishing Ltd.
ISSN:	0378-1097
Date:	November 2011
Volume:	Vol.324
Number:	No.2
Page Range:	pp. 106-110
Identification Number:	10.1111/j.1574-6968.2011.02395.x
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
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URI:	http://wrap.warwick.ac.uk/id/eprint/40320

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