We used metalloregulated luciferase reporter fusions and spectroscopic
quantification of soluble Hg(II) to determine that the hydroperoxidas
e-catalase, KatG, of Escherichia coli can oxidize monatomic elemental
mercury vapor, Hg(0), to the water-soluble, ionic form, Hg(II). A stra
in with a mutation in katG and a strain overproducing KatG were used t
o demonstrate that the amount of Hg(II) formed is proportional to the
catalase activity. Hg(0) oxidation was much decreased in stationary-ph
ase cells of a strain lacking KatG, suggesting that the monofunctional
hydroperoxide 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 t
his reaction. Two typical soil bacteria, Bacillus and Streptomyces, al
so oxidize Hg(0) to Hg(II). These observations establish for the first
time that bacteria can contribute, as do mammals and plants, to the o
xidative phase of the global Hg cycle.