histidine has been researched along with ubiquinol in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (20.00) | 18.7374 |
1990's | 1 (20.00) | 18.2507 |
2000's | 3 (60.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Miki, T; Yu, CA; Yu, L | 1 |
Fang, H; Gennis, RB; Lin, RJ | 1 |
Barquera, B; Gennis, RB; Hellwig, P | 1 |
Bertero, MG; Blasco, F; Boroumand, N; Ginet, N; Palak, M; Rothery, RA; Strynadka, NC; Weiner, JH | 1 |
Mulkidjanian, AY | 1 |
1 review(s) available for histidine and ubiquinol
Article | Year |
---|---|
Ubiquinol oxidation in the cytochrome bc1 complex: reaction mechanism and prevention of short-circuiting.
Topics: Catalytic Domain; Electron Transport; Electron Transport Complex III; Glutamine; Histidine; Models, Biological; Oxidation-Reduction; Ubiquinone | 2005 |
4 other study(ies) available for histidine and ubiquinol
Article | Year |
---|---|
Hematoporphyrin-promoted photoinactivation of mitochondrial ubiquinol-cytochrome c reductase: selective destruction of the histidine ligands of the iron-sulfur cluster and protective effect of ubiquinone.
Topics: Animals; Cattle; Electron Spin Resonance Spectroscopy; Electron Transport Complex III; Hematoporphyrins; Histidine; Iron-Sulfur Proteins; Kinetics; Light; Mitochondria, Heart; Spectrophotometry; Superoxide Dismutase; Time Factors; Ubiquinone | 1991 |
Location of heme axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site-directed mutagenesis.
Topics: Amino Acid Sequence; Binding Sites; Blotting, Western; Cloning, Molecular; Codon; Cytochrome b Group; Cytochromes; DNA, Bacterial; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Molecular Sequence Data; Mutation; Oxidation-Reduction; Oxidoreductases; Oxygen; Protein Conformation; Structure-Activity Relationship; Ubiquinone; Water | 1989 |
Direct evidence for the protonation of aspartate-75, proposed to be at a quinol binding site, upon reduction of cytochrome bo3 from Escherichia coli.
Topics: Amides; Aspartic Acid; Binding Sites; Cytochrome b Group; Cytochromes; Electrochemistry; Electron Transport Complex IV; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Histidine; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Protons; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Ubiquinone | 2001 |
Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A.
Topics: Binding Sites; Cell Membrane; Crystallography, X-Ray; Dose-Response Relationship, Drug; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Histidine; Hydroxyquinolines; Kinetics; Lysine; Models, Chemical; Models, Molecular; Mutation; Naphthols; Nitrate Reductase; Nitrate Reductases; Oxidoreductases; Oxygen; Pentachlorophenol; Plasmids; Protein Binding; Protons; Terpenes; Ubiquinone | 2005 |