ABSTRACT
The iron-oxidizing bacterium Acidithiobacillus ferrooxidans MON-1 is highly resistant not only to mercuric chloride (HgCl(2)) but also to organomercurials such as methylmercury chloride (MMC). We have found that cytochrome c oxidase, purified from strain MON-1, reduces Hg(2+) to volatilizable metal mercury (Hg(0)) with reduced mammalian cytochrome c or Fe(2+) as an electron donor. In this study we found that cytochrome c oxidase can volatilize Hg(0) from MMC as well as from Hg(2+) with reduced mammalian cytochrome c or c-type cytochrome purified from strain MON-1 as an electron donor. We also found that MMC-Hg(0) volatilization activity is present in the MON-1 plasma membrane but not in the cytosol. These activities were strongly inhibited by sodium cyanide (NaCN) and the antibody produced against purified MON-1 cytochrome c oxidase. This is the first report to indicate that cytochrome c oxidase is involved in the degradation of organomercurials in microorganisms.
