Literature DB >> 6693354

Plasmid-encoded mercuric reductase in Mycobacterium scrofulaceum.

P S Meissner, J O Falkinham.   

Abstract

A Chesapeake Bay water isolate of Mycobacterium scrofulaceum containing a 115-megadalton plasmid (pVT1) grew in the presence of 100 microM HgCl2 and converted soluble 203Hg2+ to volatile mercury at a rate of 50 pmol/10(8) cells per min. Cell extracts contained a soluble mercuric reductase whose activity was not dependent on exogenously supplied thiol compounds. The enzyme displayed nearly identical activity when either NADH or NADPH served as the electron donor. A spontaneously cured derivative lacking pVT1 failed to grow in the presence of 100 microM HgCl2 and possessed no detectable mercuric reductase activity.

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Year:  1984        PMID： 6693354      PMCID： PMC215301          DOI： 10.1128/jb.157.2.669-672.1984

Source DB:  PubMed          Journal:  J Bacteriol        ISSN： 0021-9193            Impact factor:   3.490


  20 in total

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  22 in total

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10.  Development of a new generation of vectors for gene expression, gene replacement, and protein-protein interaction studies in mycobacteria.

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