Bacterial oxidation of mercury metal vapor, Hg(0).
We used metalloregulated luciferase reporter fusions and spectroscopic quantification of soluble Hg(II) to determine that the hydroperoxidase-catalase, KatG, of Escherichia coli can oxidize monatomic elemental mercury vapor, Hg(0), to the water-soluble, ionic form, Hg(II). A strain with a mutation in katG and a strain overproducing KatG were used to demonstrate that the amount of Hg(II) formed is proportional to the catalase activity. Hg(0) oxidation was much decreased in stationary-phase cells of a strain lacking KatG, suggesting that the monofunctional hydroperoxidase KatE is less effective at this reaction. Unexpectedly, Hg(0) oxidation also occurred in a strain lacking both KatE and KatG, suggesting that activities other than hydroperoxidases may carry out this reaction. Two typical soil bacteria, Bacillus and Streptomyces, also oxidize Hg(0) to Hg(II). These observations establish for the first time that bacteria can contribute, as do mammals and plants, to the oxidative phase of the global Hg cycle.
Smith
T
T
Department of Microbiology, University of Georgia, Athens 30602-2605, USA.
Pitts
K
K
McGarvey
J A
JA
Summers
A O
AO
D019677:Artificial Gene Fusion; D001426:Bacterial Proteins; D002374:Catalase / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D005798:Genes, Bacterial; D017930:Genes, Reporter; D008156:Luciferases / Q000235:genetics; D008628:Mercury / Q000378:metabolism*; D009154:Mutation; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000235:genetics / Q000378:metabolism; D012988:Soil Microbiology
D001426:Bacterial Proteins; D010544:Peroxidases; C102664:hydroperoxidase II; D002374:Catalase; C076136:catalase HPI; D008156:Luciferases; D008628:Mercury