Reduction of Hg2+ with Reduced Mammalian Cytochrome c by Cytochrome c Oxidase Purified from a Mercury-Resistant Acidithiobacillus ferrooxidans Strain, MON-1

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  • SUGIO Tsuyoshi
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
  • FUJII Mitsuko
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
  • NINOMIYA Yumika
    Department of Biological Function, Faculty of Agriculture, Okayama University
  • KANAO Tadayoshi
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
  • NEGISHI Atsunori
    Technical Research Institute, Hazama Corporation
  • TAKEUCHI Fumiaki
    Environmental Management Center, Okayama University

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  • Reduction of Hg<sup>2+</sup>with Reduced Mammalian Cytochrome<i>c</i>by Cytochrome<i>c</i>Oxidase Purified from a Mercury-Resistant<i>Acidithiobacillus ferrooxidans</i>Strain, MON-1

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Acidithiobacillus ferrooxidans AP19-3, ATCC 23270, and MON-1 are mercury-sensitive, moderately mercury-resistant, and highly mercury-resistant strains respectively. It is known that 2,3,5,6-tetramethyl-p-phenylendiamine (TMPD) and reduced cytochrome c are used as electron donors specific for cytochrome c oxidase. Resting cells of strain MON-1 had TMPD oxidase activity and volatilized metal mercury with TMPD as an electron donor. Cytochrome c oxidase purified from strain MON-1 reduced mercuric ions to metalic mercury with reduced mammalian cytochrome c as well as TMPD. These mercury volatilization activities with reduced cytochrome c and TMPD were completely inhibited by 1 mM NaCN. These results indicate that cytochrome c oxidase is involved in mercury reduction in A. ferrooxidans cells. The cytochrome c oxidase activities of strains AP19-3 and ATCC 23270 were completely inhibited by 1 μM and 5 μM of mercuric chloride respectively. In contrast, the activity of strain MON-1 was inhibited 33% by 5 μM, and 70% by 10 μM of mercuric chloride, suggesting that the levels of mercury resistance in A. ferrooxidans strains correspond well with the levels of mercury resistance of cytochrome c oxidase.

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