Response to mercury (II) ions in Methylococcus capsulatus (Bath)
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 0378-1097Full text not available from this repository.
Official URL: http://dx.doi.org/10.1111/j.1574-6968.2011.02395.x
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 22.214.171.124). 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.
|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.|
|Page Range:||pp. 106-110|
|Access rights to Published version:||Restricted or Subscription Access|
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