Factors determining electron-transfer rates in cytochrome c oxidase: investigation of the oxygen reaction in the R. sphaeroides enzyme.
暂无分享,去创建一个
[1] G. Babcock,et al. Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[2] H. Rottenberg. The generation of proton electrochemical potential gradient by cytochrome c oxidase. , 1998, Biochimica et biophysica acta.
[3] R. Gennis,et al. Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides. , 1998, Biochemistry.
[4] P. Brzezinski,et al. Pathways of Proton Transfer in Cytochrome c Oxidase , 1998, Journal of bioenergetics and biomembranes.
[5] R. Gennis,et al. Glutamate 286 in cytochrome aa3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen. , 1997, Biochemistry.
[6] R. Gennis,et al. Factors determining electron-transfer rates in cytochrome c oxidase: studies of the FQ(I-391) mutant of the Rhodobacter sphaeroides enzyme. , 1997, Biochemistry.
[7] H. Michel,et al. Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[8] R. Gennis,et al. The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[9] P. Brzezinski,et al. Oxidation of ubiquinol by cytochrome bo3 from Escherichia coli: kinetics of electron and proton transfer. , 1997, Biochemistry.
[10] O Einarsdóttir,et al. Mechanism of cytochrome c oxidase-catalyzed reduction of dioxygen to water: evidence for peroxy and ferryl intermediates at room temperature. , 1997, Biochemistry.
[11] S. Papa,et al. Redox-linked protolytic reactions in soluble cytochrome-c oxidase from beef-heart mitochondria: redox Bohr effects. , 1997, Biochimica et biophysica acta.
[12] A. Puustinen,et al. The "ferrous-oxy" intermediate in the reaction of dioxygen with fully reduced cytochromes aa3 and bo3. , 1996, Biochemistry.
[13] S. Ferguson-Miller,et al. Heme/Copper Terminal Oxidases. , 1996, Chemical reviews.
[14] M. Wikström,et al. Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase. , 1996, Biochemistry.
[15] T. Tomizaki,et al. The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å , 1996, Science.
[16] C. A. James,et al. Flow-flash kinetics of O2 binding to cytochrome c oxidase at elevated [O2]: observations using high pressure stopped flow for gaseous reactants. , 1996, Biochemical and biophysical research communications.
[17] T. Tomizaki,et al. Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A , 1995, Science.
[18] Hartmut Michel,et al. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans , 1995, Nature.
[19] M. Wikström,et al. Structure of CuB in the binuclear heme-copper center of the cytochrome aa3-type quinol oxidase from Bacillus subtilis: an ENDOR and EXAFS study. , 1995, Biochemistry.
[20] R. Gennis,et al. Rapid purification of wildtype and mutant cytochrome c oxidase from Rhodobacter sphaeroides by Ni2+‐NTA affinity chromatography , 1995, FEBS letters.
[21] M. Wikström,et al. Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: a role for protons. , 1995, Biochemistry.
[22] P. Brzezinski,et al. Internal electron transfer in cytochrome c oxidase from Rhodobacter sphaeroides. , 1995, Biochemistry.
[23] I. W. Levin,et al. Near infrared spectral changes of cytochrome aa3 during potentiometric titrations. , 1994, Biophysical journal.
[24] S. Yoshikawa,et al. Selective resonance Raman observation of the "607 nm" form generated in the reaction of oxidized cytochrome c oxidase with hydrogen peroxide. , 1994, The Journal of biological chemistry.
[25] R. Gennis,et al. The cytochrome oxidase superfamily of redox-driven proton pumps. , 1994, Trends in biochemical sciences.
[26] P. Rich,et al. Proton uptake by cytochrome c oxidase on reduction and on ligand binding. , 1994, Biochimica et biophysica acta.
[27] M. Wikström,et al. Oxygen binding and activation: early steps in the reaction of oxygen with cytochrome c oxidase. , 1994, Biochemistry.
[28] P. Brzezinski,et al. Light-induced structural changes in cytochrome c oxidase: implication for the mechanism of electron and proton gating. , 1994, Biochimica et biophysica acta.
[29] S. Ferguson-Miller,et al. Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase. Purification, kinetics, proton pumping, and spectral analysis. , 1992, The Journal of biological chemistry.
[30] T. Nilsson,et al. Proton transfer during the reaction between fully reduced cytochrome c oxidase and dioxygen: pH and deuterium isotope effects. , 1992, Biochemistry.
[31] M. Wikström,et al. The dioxygen cycle. Spectral, kinetic, and thermodynamic characteristics of ferryl and peroxy intermediates observed by reversal of the cytochrome oxidase reaction. , 1992, The Journal of biological chemistry.
[32] G. Babcock,et al. Oxygen activation and the conservation of energy in cell respiration , 1992, Nature.
[33] B. Hill. The reaction of the electrostatic cytochrome c-cytochrome oxidase complex with oxygen. , 1991, The Journal of biological chemistry.
[34] M. Oliveberg,et al. Uptake and release of protons during the reaction between cytochrome c oxidase and molecular oxygen: a flow-flash investigation. , 1991, Biochemistry.
[35] D. Rousseau,et al. Ferryl and hydroxy intermediates in the reaction of oxygen with reduced cytochrome c oxidase , 1990, Nature.
[36] D. Rousseau,et al. Cytochrome c oxidase: decay of the primary oxygen intermediate involves direct electron transfer from cytochrome a. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[37] M. Oliveberg,et al. The effect of pH and temperature on the reaction of fully reduced and mixed-valence cytochrome c oxidase with dioxygen. , 1989, Biochimica et biophysica acta.
[38] H. Schägger,et al. Purification of cytochrome-c oxidase retaining its pulsed form. , 1989, European journal of biochemistry.
[39] M. Wikström. Identification of the electron transfers in cytochrome oxidase that are coupled to proton-pumping , 1989, Nature.
[40] M. Wikström. Pumping of protons from the mitochondrial matrix by cytochrome oxidase , 1984, Nature.
[41] B. Hill,et al. The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature. Evidence for new pathways of electron transfer. , 1984, The Biochemical journal.
[42] B. Hill,et al. Spectroscopic evidence for the participation of compound A (Fea32+-O2) in the reaction of mixed-valence cytochrome c oxidase with oxygen at room temperature. , 1983, The Biochemical journal.
[43] I. Pecht,et al. Conformational equilibria accompanying the electron transfer between cytochrome c (P551) and azurin from Pseudomonas aeruginosa. , 1976, Biochemistry.
[44] B Chance,et al. Functional intermediates in the reaction of membrane-bound cytochrome oxidase with oxygen. , 1975, The Journal of biological chemistry.
[45] W. Vanneste. The stoichiometry and absorption spectra of components a and a-3 in cytochrome c oxidase. , 1966, Biochemistry.
[46] C. Greenwood,et al. Reactions of cytochrome oxidase with oxygen and carbon monoxide. , 1963, The Biochemical journal.
[47] R. Gennis,et al. Energy Transduction by Cytochrome Complexes in Mitochondrial and Bacterial Respiration: The Enzymology of Coupling Electron Transfer Reactions to Transmembrane Proton Translocation , 1994 .
[48] G. Babcock,et al. Resolution of the reaction sequence during the reduction of O2 by cytochrome oxidase. , 1993, Proceedings of the National Academy of Sciences of the United States of America.