Nitric oxide-reductase homologue that contains a copper atom and has cytochrome c-oxidase activity from an aerobic phototrophic bacterium Roseobacter denitrificans

Yuji Matsuda, Kei Ichiro Inamori, Tsukasa Osaki, Akane Eguchi, Azusa Watanabe, Shun-Ichiro Kawabata, Koh Iba, Hiroyuki Arata

研究成果: ジャーナルへの寄稿記事

15 引用 (Scopus)

抄録

A cytochrome cb-type enzyme with cytochrome c-oxidase activity was purified from an aerobic phototrophic bacterium Roseobacter denitrificans. The enzyme was solubilized with sucrose monodecanoate from the membranes of R. denitrificans grown aerobically under light conditions, and purified to electrophoretic homogeneity. Absorption spectra of the purified enzyme showed peaks at 410 nm and 530 nm in the oxidized state, and peaks at 420, 522, and 551 nm and a shoulder at around 560 nm in the reduced state. The enzyme is composed of two subunits with apparent molecular weights on SDS-PAGE of 37,000 and 18,000, the latter positive to heme staining. The protein contains heme c, heme b, and copper in a 1:2:1 stoichiometry. The spectral properties indicated that the heme c and one heme b are in low-spin states, while the other heme b is in a high-spin state. The base sequences of the genes and the deduced amino acid sequences are similar to those of known NorB and NorC subunits of nitric oxide reductases from other bacterial species. The enzyme is similar to nitric oxide reductase, but differs in that it contains copper. Virtually no nitric oxide reductase activity was detected in the purified enzyme.

元の言語英語
ページ(範囲)791-800
ページ数10
ジャーナルJournal of Biochemistry
131
発行部数6
出版物ステータス出版済み - 2002

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Roseobacter
Aerobic bacteria
Aerobic Bacteria
Electron Transport Complex IV
Heme
Copper
Atoms
Enzymes
Cytochromes
Stoichiometry
Sucrose
nitric-oxide reductase
Polyacrylamide Gel Electrophoresis
Absorption spectra
Amino Acid Sequence
Genes
Molecular Weight
Molecular weight
Staining and Labeling
Membranes

All Science Journal Classification (ASJC) codes

  • Biochemistry

これを引用

Nitric oxide-reductase homologue that contains a copper atom and has cytochrome c-oxidase activity from an aerobic phototrophic bacterium Roseobacter denitrificans. / Matsuda, Yuji; Inamori, Kei Ichiro; Osaki, Tsukasa; Eguchi, Akane; Watanabe, Azusa; Kawabata, Shun-Ichiro; Iba, Koh; Arata, Hiroyuki.

:: Journal of Biochemistry, 巻 131, 番号 6, 2002, p. 791-800.

研究成果: ジャーナルへの寄稿記事

Matsuda, Yuji ; Inamori, Kei Ichiro ; Osaki, Tsukasa ; Eguchi, Akane ; Watanabe, Azusa ; Kawabata, Shun-Ichiro ; Iba, Koh ; Arata, Hiroyuki. / Nitric oxide-reductase homologue that contains a copper atom and has cytochrome c-oxidase activity from an aerobic phototrophic bacterium Roseobacter denitrificans. :: Journal of Biochemistry. 2002 ; 巻 131, 番号 6. pp. 791-800.
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abstract = "A cytochrome cb-type enzyme with cytochrome c-oxidase activity was purified from an aerobic phototrophic bacterium Roseobacter denitrificans. The enzyme was solubilized with sucrose monodecanoate from the membranes of R. denitrificans grown aerobically under light conditions, and purified to electrophoretic homogeneity. Absorption spectra of the purified enzyme showed peaks at 410 nm and 530 nm in the oxidized state, and peaks at 420, 522, and 551 nm and a shoulder at around 560 nm in the reduced state. The enzyme is composed of two subunits with apparent molecular weights on SDS-PAGE of 37,000 and 18,000, the latter positive to heme staining. The protein contains heme c, heme b, and copper in a 1:2:1 stoichiometry. The spectral properties indicated that the heme c and one heme b are in low-spin states, while the other heme b is in a high-spin state. The base sequences of the genes and the deduced amino acid sequences are similar to those of known NorB and NorC subunits of nitric oxide reductases from other bacterial species. The enzyme is similar to nitric oxide reductase, but differs in that it contains copper. Virtually no nitric oxide reductase activity was detected in the purified enzyme.",
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AU - Matsuda, Yuji

AU - Inamori, Kei Ichiro

AU - Osaki, Tsukasa

AU - Eguchi, Akane

AU - Watanabe, Azusa

AU - Kawabata, Shun-Ichiro

AU - Iba, Koh

AU - Arata, Hiroyuki

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N2 - A cytochrome cb-type enzyme with cytochrome c-oxidase activity was purified from an aerobic phototrophic bacterium Roseobacter denitrificans. The enzyme was solubilized with sucrose monodecanoate from the membranes of R. denitrificans grown aerobically under light conditions, and purified to electrophoretic homogeneity. Absorption spectra of the purified enzyme showed peaks at 410 nm and 530 nm in the oxidized state, and peaks at 420, 522, and 551 nm and a shoulder at around 560 nm in the reduced state. The enzyme is composed of two subunits with apparent molecular weights on SDS-PAGE of 37,000 and 18,000, the latter positive to heme staining. The protein contains heme c, heme b, and copper in a 1:2:1 stoichiometry. The spectral properties indicated that the heme c and one heme b are in low-spin states, while the other heme b is in a high-spin state. The base sequences of the genes and the deduced amino acid sequences are similar to those of known NorB and NorC subunits of nitric oxide reductases from other bacterial species. The enzyme is similar to nitric oxide reductase, but differs in that it contains copper. Virtually no nitric oxide reductase activity was detected in the purified enzyme.

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