Existence of Ferrous Iron-Dependent Mercury Reducing Enzyme System in Sulfur-Grown A. Ferrooxidans MON-1 Cells

Article Preview

Abstract:

Iron-grown Acidithiobacillus ferrooxidans MON-1 cells are highly resistant to organomercurial compounds as well as mercuric chloride (HgCl2). Existence of a novel Hg2+-reducing enzyme system, in which mercury resistant aa3-type cytochrome c oxidase catalyzes the reduction of Hg2+ with reduced mammalian cytochrome c or Fe2+ as an electron donor to give Hg0, has been shown in iron-grown MON-1 cells. There has been no reports on the mechanism of Hg2+ reduction by sulfur-grown A. ferrooxidans cells. The level of mercury resistance in sulfur-grown A. ferrooxidans MON-1 cells was compared with that of iron-grown MON-1 cells. Strain MON-1 was able to grow in 1% elemental sulfur medium (pH 2.5) containing 10 μM of Hg2+ or 0.2 μM phenylmercury acetate (PMA), suggesting that the levels of mercury resistance to inorganic and organic mercurial compounds are nearly the same in iron- and sulfur-grown MON-1 cells. Activity levels of Hg0 volatilization from HgCl2, PMA, and methylmercury chloride (MMC) were also nearly the same in iron- and sulfur-grown cells and these activities were markedly activated by 100 mM of Fe2+, but strongly inhibited by 1 mM of sodium cyanide, indicating that sulfur-grown MON-1 cells has the activity of ferrous iron-dependent mercury reducing enzyme system containing aa3-type cytochrome oxidase. aa3-type cytochrome c oxidase purified partially from sulfur-grown MON-1 cells showed both the iron oxidase and mercury reductase activities in the presence, but not in the absence, of rusticyanin and c-type cytochromes (Cyc1 and Cyc2) partially purified from iron-grown MON-1 cells.

You might also be interested in these eBooks

Info:

Periodical:

Advanced Materials Research (Volumes 71-73)

Pages:

745-748

Citation:

Online since:

May 2009

Export:

Price:

Permissions CCC:

Permissions PLS:

Сopyright:

© 2009 Trans Tech Publications Ltd. All Rights Reserved

Share:

Citation:

[1] G. J. Olson, F. D. Porter, J. Rubinstein, and S. Silver: J. Bacteriol., 151 (1982), p.1230.

Google Scholar

[2] F. Takeuchi, K. Iwahori, K. Kamimura, and T. Sugio: J. Biosci. Bioeng., 88 (1999), p.387.

Google Scholar

[3] D. G. Rawlings, and T. Kusano: Microbiol. Rev., 58 (1994), p.39.

Google Scholar

[4] T. Sugio, M. Fujii, F. Takeuchi, A. Negishi, T. Maeda, and K. Kamimura: Biosci. Biotechnol. Biochem., 67 (2003), p.1537.

Google Scholar

[5] K. Iwahori, F. Takeuchi, K. Kamimura, and T. Sugio: Appl. Environ. Microbiol., 66, (2000), p.3823.

Google Scholar

[6] T. Sugio, K. Iwahori, F. Takeuchi, A. Negishi, T. Maeda, and K. Kamimura: J. Biosci. Bioeng., 92 (2001), p.44.

DOI: 10.1263/jbb.92.44

Google Scholar

[7] T. Sugio, M. Fujii, Y. Ninomiya, T. Kanao, A. Negishi, and F. Takeuchi: Biosci. Biotechnol. Biochem., 72 (2008), p.2756.

Google Scholar

[8] T. M. Taha, T. Kanao, F. Takeuchi, and T. Sugio: Appl. Environ. Microbiol., 74 (2008), p.6808.

Google Scholar

[9] F. Takeuchi, A. Negishi, S. Nakamura, T. Kanao, K. Kamimura, and T. Sugio: J. Biosci. Bioeng., 99 (2005), p.586.

Google Scholar