Mogi T | Univ. Tokyo Tokyo
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概要
関連著者
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Mogi T
Univ. Tokyo Tokyo
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Mogi Tatsushi
Chemical Resources Laboratory Tokyo Institute Of Technology
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Mogi Tatsushi
Department Of Biological Science Graduate School Of Science The University Of Tokyo
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Hori Hitoshi
Biotechnology Research Laboratory Tosoh Co.
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TSUBAKI Motonari
Department of Life Science, Faculty of Science, Himeji Institute of Technology
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Hori H
Nagoya Univ. Nagoya Jpn
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Tsubaki M
Department Of Chemistry Graduate School Of Science Kobe University
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Tsubaki Motonari
Department Of Life Science Faculty Of Science Himeji Institute Of Technology
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Tsubaki Motonari
Department Of Chemistry Graduate School Of Science Kobe University
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Tsubaki Motonari
Departmemt of Chemistiy, Graduate School of Science, Kobe University
著作論文
- Kinetic Mechanism of Quinol Oxidation by Cytochrome bd Studied with Ubiquinone-2 Analogs
- Azide- and Cyanide-Binding to the Escherichia coli bd-Type Ubiquinol Oxidase Studied by Visible Absorption, EPR and FTIR Spectroscopies
- Effects of Subunit I Mtations on Redox-Linked Conformational Changes of the Escherichia coli bo-type Ubiquinol Oxidase Revealed by Fourier-Transform Infrared Spectroscopy^1
- Fluoride-Binding to the Escherichia coli bd-Type Ubiquinol Oxidase Strdied by Visible Absorption and EPR Sdpectroscopies^1
- Fourier-Transform Infrared Studies on Conformation Changes in bd-Type Ubiquinol Oxidase from Escherichia coli upon Photoreduction of the Redox Metal Centers^1
- Characterization of the Ubiquinol Oxidation Sites in Cytochromes bo and bd from Escherichia coli using Aurachin C Analogues
- Expression of the Escherichia coli bo-Type Ubiquinol Oxidase with a Chimeric Subunit II Having the Cu_A-Cytochrome c Domain from the Thermophilic Bacillus caa_3-Type Cytochrome c Oxidase
- A Novel Chloride-Binding Site Modulates the Heme-Copper Binuclear Center of the Escherichia coli bo-Type Ubiquinol Oxidase