Cytochrome c oxidase purified from a mercury-resistant strain of Acidithiobacillus ferrooxidans volatilizes mercury

Tsuyoshi Sugio, Kenji Iwahori, Fumiaki Takeuchi, Atsunori Negishi, Terunobu Maeda, Kazuo Kamimura

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

We suggested in our previous study that the plasma membrane cytochrome c oxidase of the mercury-resistant iron-oxidizing bacterial strain Acidithiobacillus ferrooxidans, SUG 2-2, is involved in Fe2+-dependent mercury volatilization. To study the involvement of A. ferrooxidans cytochrome c oxidase in mercury reduction, the cytochrome c oxidase was extracted from mercury-resistant and mercury-sensitive strains and purified. The Fe2+-dependent mercury volatilization activities of the oxidases from these strains were compared. The cytochrome c oxidase from strain SUG 2-2 volatilized 39% of the total Hg2+ (7 nmol) that had been added to a 10-li reaction mixture (pH 3.8) in the presence of 10 μmol of Fe2+ after a 7-d incubation period at 30°C. In contrast, the enzyme purified from the mercury-sensitive strain AP19-3 volatilized 3.5% of the total mercury under the same conditions. The boiled SUG 2-2 oxidase did not exhibit activity to volatilize mercury. Fe2+ reduced the oxidase from SUG 2-2 and Hg2+ oxidized the reduced enzyme. The purified SUG 2-2 oxidase is composed of three protein subunits with apparent molecular weights of 56,000 Da (α), 24,000 Da (β), and 19,000 Da (γ). The amount of mercury bound to the purified SUG 2-2 oxidase was 6.2 μg/mg protein and those bound to α-, β- and γ-subunits of the cytochrome c oxidase were 3.5, 2.6 and 0.7 μg/mg protein, respectively.

Original languageEnglish
Pages (from-to)44-49
Number of pages6
JournalJournal of Bioscience and Bioengineering
Volume92
Issue number1
DOIs
Publication statusPublished - 2001

Fingerprint

Acidithiobacillus
Electron Transport Complex IV
Mercury
Oxidoreductases
Proteins
Vaporization
Enzymes
Volatilization
Mercury (metal)
Cell membranes
Molecular weight
Iron
Protein Subunits

Keywords

  • Acidithiobacillus ferrooxidans
  • Cytochrome c oxidase
  • Iron-oxidizing bacteria
  • Mercury resistance
  • Mercury volatilization

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering

Cite this

Cytochrome c oxidase purified from a mercury-resistant strain of Acidithiobacillus ferrooxidans volatilizes mercury. / Sugio, Tsuyoshi; Iwahori, Kenji; Takeuchi, Fumiaki; Negishi, Atsunori; Maeda, Terunobu; Kamimura, Kazuo.

In: Journal of Bioscience and Bioengineering, Vol. 92, No. 1, 2001, p. 44-49.

Research output: Contribution to journalArticle

Sugio, Tsuyoshi ; Iwahori, Kenji ; Takeuchi, Fumiaki ; Negishi, Atsunori ; Maeda, Terunobu ; Kamimura, Kazuo. / Cytochrome c oxidase purified from a mercury-resistant strain of Acidithiobacillus ferrooxidans volatilizes mercury. In: Journal of Bioscience and Bioengineering. 2001 ; Vol. 92, No. 1. pp. 44-49.
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AU - Sugio, Tsuyoshi

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AU - Maeda, Terunobu

AU - Kamimura, Kazuo

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N2 - We suggested in our previous study that the plasma membrane cytochrome c oxidase of the mercury-resistant iron-oxidizing bacterial strain Acidithiobacillus ferrooxidans, SUG 2-2, is involved in Fe2+-dependent mercury volatilization. To study the involvement of A. ferrooxidans cytochrome c oxidase in mercury reduction, the cytochrome c oxidase was extracted from mercury-resistant and mercury-sensitive strains and purified. The Fe2+-dependent mercury volatilization activities of the oxidases from these strains were compared. The cytochrome c oxidase from strain SUG 2-2 volatilized 39% of the total Hg2+ (7 nmol) that had been added to a 10-li reaction mixture (pH 3.8) in the presence of 10 μmol of Fe2+ after a 7-d incubation period at 30°C. In contrast, the enzyme purified from the mercury-sensitive strain AP19-3 volatilized 3.5% of the total mercury under the same conditions. The boiled SUG 2-2 oxidase did not exhibit activity to volatilize mercury. Fe2+ reduced the oxidase from SUG 2-2 and Hg2+ oxidized the reduced enzyme. The purified SUG 2-2 oxidase is composed of three protein subunits with apparent molecular weights of 56,000 Da (α), 24,000 Da (β), and 19,000 Da (γ). The amount of mercury bound to the purified SUG 2-2 oxidase was 6.2 μg/mg protein and those bound to α-, β- and γ-subunits of the cytochrome c oxidase were 3.5, 2.6 and 0.7 μg/mg protein, respectively.

AB - We suggested in our previous study that the plasma membrane cytochrome c oxidase of the mercury-resistant iron-oxidizing bacterial strain Acidithiobacillus ferrooxidans, SUG 2-2, is involved in Fe2+-dependent mercury volatilization. To study the involvement of A. ferrooxidans cytochrome c oxidase in mercury reduction, the cytochrome c oxidase was extracted from mercury-resistant and mercury-sensitive strains and purified. The Fe2+-dependent mercury volatilization activities of the oxidases from these strains were compared. The cytochrome c oxidase from strain SUG 2-2 volatilized 39% of the total Hg2+ (7 nmol) that had been added to a 10-li reaction mixture (pH 3.8) in the presence of 10 μmol of Fe2+ after a 7-d incubation period at 30°C. In contrast, the enzyme purified from the mercury-sensitive strain AP19-3 volatilized 3.5% of the total mercury under the same conditions. The boiled SUG 2-2 oxidase did not exhibit activity to volatilize mercury. Fe2+ reduced the oxidase from SUG 2-2 and Hg2+ oxidized the reduced enzyme. The purified SUG 2-2 oxidase is composed of three protein subunits with apparent molecular weights of 56,000 Da (α), 24,000 Da (β), and 19,000 Da (γ). The amount of mercury bound to the purified SUG 2-2 oxidase was 6.2 μg/mg protein and those bound to α-, β- and γ-subunits of the cytochrome c oxidase were 3.5, 2.6 and 0.7 μg/mg protein, respectively.

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