Involvement of Cytochrome a in Iron Oxidation of a Moderately Thermophilic Iron-Oxidizing Bacterium, Strain TI-1
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概要
- 論文の詳細を見る
The iron-oxidizing activity of a moderately thermophilic iron-oxidizing bacterium, strain TI-1,was located in the plasma membrane. When the strain was grown in Fe^<2+> (60mM)-salts medium containing yeast extract (0.03%), the plasma membrane had iron-oxidizing activity of 0.129μmol O_2 uptake/mg/min. Iron oxidase was solubilized from the plasma membrane with 1.0% n-octyl-β-D-glucopyranoside (OGL) containing 25% (v/v) glycerol (pH 3.0) and purified 37-fold by a SP Sepharose FF column chromatography. Iron oxidase solubilized from the plasma membrane was stable at pH 3.0,but quite unstable in the buffer with the pH above 6.0 or below 1.0. The optimum pH and temperature for iron oxidation were 3.0 and 55℃, respectively. Solubilized enzyme from the membrane showed absorption peaks characteristic of cytochromes a and b. Cyanide and azide, inhibitors of cytochrome c oxidase, completely inhibited iron-oxidizing activity at 100μM, but antimycin A, 2-n-heptyl-4-hydroxyquinoline-N-oxide (HOQNO) and myxothiazol, inhibitors of electron transport systems involved with cytochrome b, did not inhibit enzyme activity at 10 μM. The absorption spectrum of the most active enzyme fraction from SP Sepharose FF column chromatography (4.76 μmol O_2 uptake/mg/min) compared with lower active fractions from the chromatography (0.009 and 2.10 μmol O_2 uptake/mg/min) showed a large α-peak of cytochrome a at 602 nm and a smaller α-peak of cytochrome b at 560 nm. The absorption spectrum of pyridine ferrohemochrome prepared from the most highly purified enzyme showed an α-peak characteristic of heme a at 587 nm, but not the α-peak characteristic of heme c at 550nm. The cytochrome a, but not cytochrome b, in the most highly purified enzyme fraction was reduced by the addition of ferrous iron at pH 3.0,indicating that electrons from Fe^<2+> were transported to cytochrome a, but not cytochrome b. These results strongly suggest that cytochrome a, but not cytochromes b and c, is involved in iron oxidation of strain TI-1.
- 社団法人日本農芸化学会の論文
- 1999-09-23
著者
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Kamimura Kazuo
Graduate School of Natural Science and Technology, Okayama University
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Sugio Tsuyoshi
Department of Botany and Microbiology, Division of Bioscience, Graduate School of Natural Science an
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Kamimura Kazuo
Department of Botany and Microbiology, Division of Bioscience, Graduate School of Natural Science an
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Sugio Tsuyoshi
Division Of Biological Function And Genetic Resources Science Faculty Of Agriculture Okayama Univers
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Sugio Tsuyoshi
Department Of Agricultural Chemistry Faculty Of Agriculture Okayama University
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Sugio Tsuyoshi
Department Of Biological Function And Genetic Resources Science Okayama University
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TAKAI MASAKI
Department of Biological Function and Genetic Resources Science, Faculty of Agriculture, Okayama Uni
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Kamimura K
Graduate School Of Natural Science And Technology Okayama University
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Kamimura Kazuo
Marine Biological Technology Section Chugoku National Industrial Research Institute
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Kamimura Kazuo
Department Of Biological Function And Genetic Resources Science Faculty Of Agriculture Okayama Unive
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杉尾 剛
Div. Of Bioscience Graduate School Of Natural Sci. And Technol. Okayama Univ.
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Takai M
Kobe Univ. Kobe Jpn
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Sugio T
Okayama Univ. Okayama Jpn
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Takai Masaki
Department Of Biological Function And Genetic Resources Science Faculty Of Agriculture Okayama Unive
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Kamimura Kazuo
Department Of Botany And Microbiology Division Of Bioscience Graduate School Of Natural Science And
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