Volatilization of Mercury by an Iron Oxidation Enzyme System in a Highly Mercury-resistant Acidithiobacillus ferrooxidans Strain MON-1(Microbiology & Fermentation Technology)

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概要

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• A highly mercury-resistant strain Acidithiobacillus ferrooxidans MON-1, was isolated from a culture of a moderately mercury-resistant strain, A. ferrooxidans SUG 2-2 (previously described as Thiobacillus ferrooxidans SUG 2-2), by successive cultivation and isolation of the latter strain in a Fe^<2+> medium with increased amounts of Hg^<2+> from 6 μM to 20 μM. The original stain SUG 2-2 grew in a Fe^<2+> medium containing 6μM Hg^<2+> with a lag time of 22 days, but could not grow in a Fe^<2+> medium containing 10 μM Hg^<2+>. In contrast, strain MON-1 could grow in a Fe^<2+> medium containing 20 μM Hg^<2+> with a lag time of 2 days and the ability of strain MON-1 to grow rapidly in a Fe^<2+> medium containing 20 μM Hg^<2+> was maintained stably after the strain was cultured many times in a Fe^<2+> medium without Hg^<2+>. A similar level of NADPH-dependent mercury reductase activity was observed in cell extracts from strains SUG 2-2 and MON-1. By contrast, the amounts of mercury volatilized for 3 h from the reaction mixture containing 7 μM Hg^<2+> using a Fe^<2+>-dependent mercury volatilization enzyme system were 5.6 nmol for SUG 2-2 and 67.5 nmol for MON-1, respectively, indicating that a marked increase of Fe^<2+>-dependent mercury volatilization activity conferred on strain MON-1 the ability to grow rapidly in a Fe^<2+> medium containing 20 μM Hg^<2+>. Iron oxidizing activities, 2, 3, 5, 6-tetramethyl-p-phenylenediamine (TMPD) oxidizing activities and cytochrome c oxidase activities of strains SUG 2-2 and MON-1 were 26.3 and 41.9 μl O_2 uptake/mg/min, 15.6 and 25.0 μl O_2 uptake/mg/min, and 2.1 and 6.1 mU/mg, respectively. These results indicate that among components of the iron oxidation enzyme system, especially cytochrome c oxidase activity, increased by the acquisition of further mercury resistance in strain MON-1. Mercury volatilized by the Fe^<2+>-dependent mercury volatilization enzyme system of strain MON-1 was strongly inhibited by 1.0 mM sodium cyanide, but was not by 50 nM rotenone, 5 μM 2-n-heptyl-4-hydroxyquinoline-N-oxide (HQNO), 0.5 μM antimycin A, or 0.5 μM myxothiazol, indicating that cytochrome c oxidase plays a crucial role in mercury volatilization of strain MON-1 in the presence of Fe^<2+>.

• 社団法人日本農芸化学会の論文
• 2003-07-23

著者

• TAKEUCHI Fumiaki

  Environmental Management Center, Okayama University

• Kamimura Kazuo

  Graduate School of Natural Science and Technology, Okayama University

• TAKEUCHI FUMIAKI

  Administration Center for Environmental Science and Technology, Okayama University

• 杉尾 剛

  岡山大・農

• NEGISHI Atsunori

  Technical Research Institute, Hazama Corporation

• MAEDA Terunobu

  Civil Chemical Engineering Corporation

• SUGIO Tsuyoshi

  Graduate School of Natural Science and Technology, Science and Technology for Energy Conversion, Oka

• FUJII Mitsuko

  Graduate School of Natural Science and Technology, Science and Technology for Energy Conversion, Oka

• Maeda T

  Civil Chemical Engineering Corporation

• Sugio Tsuyoshi

  Division Of Biological Function And Genetic Resources Science Faculty Of Agriculture Okayama Univers

• Sugio Tsuyoshi

  Department Of Agricultural Chemistry Faculty Of Agriculture Okayama University

• Sugio Tsuyoshi

  Department Of Biological Function And Genetic Resources Science Okayama University

• Kamimura K

  Graduate School Of Natural Science And Technology Okayama University

• Kamimura Kazuo

  Marine Biological Technology Section Chugoku National Industrial Research Institute

• Kamimura Kazuo

  Department Of Biological Function And Genetic Resources Science Faculty Of Agriculture Okayama Unive

• Maeda Toshihiro

  Applied Research Department The Chemo-sero-therapeutic Research Institute (kaketsuken)

• 杉尾 剛

  Div. Of Bioscience Graduate School Of Natural Sci. And Technol. Okayama Univ.

• Fujii Michihiko

  Kihara Inst. For Biological Res. And Graduate School Of Integrated Sci. Yokohama City Univ.

• Fujii Michihiko

  Kihara Institute For Biological Research And Graduate School Of Integrated Science Yokohama City Uni

• Takeuchi Fumiaki

  Administration Center For Environmental Science And Technology Okayama University

• Takeuchi F

  Environmental Management And Safety Section Health And Environment Center Okayama Univ.

• Takeuchi Fumiaki

  Environmental Management Center Okayama Univ.

• Sugio T

  Okayama Univ. Okayama Jpn

• Kamimura Kazuo

  Department Of Botany And Microbiology Division Of Bioscience Graduate School Of Natural Science And

• Fujii Mitsuko

  Division Of Bioscience Graduate School Of Natural Science And Technology Okayama University

• Negishi Atsunori

  Technical Research Institute Hazama Corporation

• Sugio Tsuyoshi

  Div. Of Bioscience The Graduate School Of Natural Sci. And Technol. Okayama Univ.

• Murakami Toshio

  Applied Research Department The Chemo-sero-therapeutic Research Institute (kaketsuken)

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