Assignment and Functional Roles of the cyoABCDE Gene Products Required for the Escherichia coli bo-Type Quinol Oxidase
スポンサーリンク
概要
- 論文の詳細を見る
- 1997-08-01
著者
-
MOGI Tatsushi
Department of Biological Sciences, Graduate school of Science, The University of Tokyo
-
ANRAKU Yasuhiro
Department of Biological Sciences, Graduate School of Science, University of To
-
Mogi Tatsushi
Department Of Biological Science Graduate School Of Science The University Of Tokyo
-
Nakamura Hiro
Department Of Biological Science Graduate School Of Science The University Of Tokyo
-
SAIKI Keitarou
Department of Microbiology, Nippon Dental University School of Life Dentistry at Tokyo
-
Saiki Keitarou
Department Of Biological Science Graduate School Of Science The University Of Tokyo
-
Anraku Yasuhiro
Department Of Biological Science Graduate School Of Science The University Of Tokyo
関連論文
- Biochemical and Spectroscopic Properties of Cyanide-Insensitive Quinol Oxidase from Gluconobacter oxydans
- Time-Resolved Measurements of Photovoltage Generation by Bacteriorhodopsin and Halorhodospin Adsorbed on a Thin Polymer Film
- Mitochondrial Dehydrogenases in the Aerobic Respiratory Chain of the Rodent Malaria Parasite Plasmodium yoelii yoelii
- Polymyxin B Identified as an Inhibitor of Alternative NADH Dehydrogenase and Malate : Quinone Oxidoreductase from the Gram-positive Bacterium Mycobacterium smegmatis
- Siccanin Rediscovered as a Species-Selective Succinate Dehydrogenase Inhibitor
- Signaling toward Yeast 1,3-β-glucan Synthesis
- Ca^Signal is Generated Only Once in the Mating Pheromone Response Pathway in Saccharomyces cerevisiae
- Probing the haem d-binding site in cytochrome bd quinol oxidase by site-directed mutagenesis
- Over-Expression and Characterization of Bacillus subtilis Heme O Synthase
- Probing Structure of Heme A Synthase from Bacillus subtilis by Site-Directed Mutagenesis
- Effects of Replacement of Low-Spin Haem b by Haem O on Escherichia coli Cytochromes bo and bd Quinol Oxidases
- Properties of Cytochrome bd Plastoquinol Oxidase from the Cyanobacterium Synechocystis sp. PCC 6803
- Defining the Structural Domain of Subunit II of the Heme-Copper Terminal Oxidase Using Chimeric Enzymes Constructed from the Escherichia coli bo-Type Ubiquinol Oxidase and the Thermophilic Bacillus caa_3-Type Cytochrome c Oxidase
- 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
- 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
- Substitutions of Charged Amino Acid Residues Conserved in Subunit I Perturb the Redox Metal Centers of the Escherichia coil bo-Type Ubiquinol Oxidase
- Assignment and Functional Roles of the cyoABCDE Gene Products Required for the Escherichia coli bo-Type Quinol Oxidase
- Identification of a Porphyromonas gingivalis Novel Protein Sov Required for the Secretion of Gingipains
- Deletion and Purification Studies to Elucidate the Structure of the Actinobacillus actinomycetemcomitans Cytolethal Distending Toxin
- Reconstitution and Purification of Cytolethal Distending Toxin of Actinobacillus actinomycetemcomitans
- Thirty-Three Years of The Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB) (1972-2005)
- Diversity in mitochondrial metabolic pathways in parasitic protists Plasmodium and Cryptosporidium
- Fluoride-Binding to the Escherichia coli bd-Type Ubiquinol Oxidase Studied by Visible Absorption and EPR Spectroscopies.
- Characterization of the Ubiquinol Oxidation Sites in Cytochromes bo and bd from Escherichia coli using Aurachin C Analogues.