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.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Boden R,Murrell JCdoi
10.1111/j.1574-6968.2011.02395.xsubject
Has Abstractpub_date
2011-11-01 00:00:00pages
106-10issue
2eissn
0378-1097issn
1574-6968journal_volume
324pub_type
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