Page last updated: 2024-08-23

heme and ubiquinone 8

heme has been researched along with ubiquinone 8 in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (33.33)18.2507
2000's1 (16.67)29.6817
2010's2 (33.33)24.3611
2020's1 (16.67)2.80

Authors

AuthorsStudies
Anraku, Y; Itoh, S; Matsuura, K; Miyoshi, H; Mogi, T; Sato-Watanabe, M1
Miyoshi, H; Mogi, T; Orii, Y; Sato-Watanabe, M1
Hori, H; Ishimori, K; Matsuura, K; Mogi, T; Morishima, I; Takahashi, S; Yoshioka, S1
Eisinger, ML; Gennis, RB; Hahn, A; Hellwig, P; Kühlbrandt, W; Langer, JD; Meier-Credo, J; Melin, F; Michel, H; Mills, DJ; Miyoshi, H; Nikolaev, A; Radloff, M; Safarian, S; Sakamoto, J1
Böttcher, B; Burschel, S; Friedrich, T; Kägi, J; Müller, R; Rasmussen, T; Theßeling, A; Wohlwend, D1
Chan, CK; Choi, SK; Clarke, O; Ding, Z; Gennis, R; Han, L; Hong, S; Li, J; Liu, B; Luo, Y; Tajkhorshid, E; Vallese, F; Zhang, K; Zhu, J1

Other Studies

6 other study(ies) available for heme and ubiquinone 8

ArticleYear
Stabilization of a semiquinone radical at the high-affinity quinone-binding site (QH) of the Escherichia coli bo-type ubiquinol oxidase.
    FEBS letters, 1995, Oct-30, Volume: 374, Issue:2

    Topics: Benzoquinones; Binding Sites; Coenzymes; Electron Spin Resonance Spectroscopy; Electron Transport; Electron Transport Complex IV; Enzyme Stability; Escherichia coli; Heme; Hydrogen-Ion Concentration; Oxidation-Reduction; Potentiometry; Spectrum Analysis; Ubiquinone

1995
Role of a bound ubiquinone on reactions of the Escherichia coli cytochrome bo with ubiquinol and dioxygen.
    FEBS letters, 1999, Aug-20, Volume: 457, Issue:1

    Topics: Catalysis; Cytochrome b Group; Cytochromes; Escherichia coli; Escherichia coli Proteins; Heme; Oxidation-Reduction; Oxidoreductases; Oxygen; Spectrum Analysis, Raman; Time Factors; Ubiquinone

1999
Dioxygen reduction by bo-type quinol oxidase from Escherichia coli studied by submillisecond-resolved freeze-quench EPR spectroscopy.
    Biochemistry, 2004, Mar-02, Volume: 43, Issue:8

    Topics: Binding Sites; Coenzymes; Cytochrome b Group; Electron Spin Resonance Spectroscopy; Escherichia coli Proteins; Free Radicals; Freezing; Heme; Nanotechnology; Oxidation-Reduction; Oxidoreductases; Oxygen; Spectrophotometry; Ubiquinone

2004
Active site rearrangement and structural divergence in prokaryotic respiratory oxidases.
    Science (New York, N.Y.), 2019, 10-04, Volume: 366, Issue:6461

    Topics: Catalytic Domain; Cryoelectron Microscopy; Cytochrome b Group; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Heme; Models, Molecular; Oxidation-Reduction; Oxidoreductases; Oxygen; Protein Structure, Quaternary; Protein Subunits; Protons; Ubiquinone

2019
Homologous bd oxidases share the same architecture but differ in mechanism.
    Nature communications, 2019, 11-13, Volume: 10, Issue:1

    Topics: Cytochrome b Group; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Geobacillus; Heme; Models, Molecular; Oxidoreductases; Oxygen; Protons; Sequence Homology, Amino Acid; Substrate Specificity; Ubiquinone; Water

2019
Cryo-EM structures of
    Proceedings of the National Academy of Sciences of the United States of America, 2021, 08-24, Volume: 118, Issue:34

    Topics: Binding Sites; Cryoelectron Microscopy; Cytochrome b Group; Escherichia coli; Escherichia coli Proteins; Heme; Oxidation-Reduction; Phospholipids; Protein Conformation; Proton Pumps; Ubiquinone

2021