Energetics of quinone-dependent electron and proton transfers in Rhodobacter sphaeroides photosynthetic reaction centers.
暂无分享,去创建一个
[1] E. Martin,et al. Modulation of the free energy of the primary quinone acceptor (QA) in reaction centers from Rhodobacter sphaeroides: contributions from the protein and protein-lipid(cardiolipin) interactions. , 2004, Biochimica et biophysica acta.
[2] S. Iwata,et al. Variation in proton donor/acceptor pathways in succinate:quinone oxidoreductases , 2003, FEBS letters.
[3] D. Kleinfeld,et al. Electron-transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: evidence for light-induced structural changes. , 1984, Biochemistry.
[4] M. Karplus,et al. pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model. , 1990, Biochemistry.
[5] G. Feher,et al. Proton and electron transfer in bacterial reaction centers. , 2000, Biochimica et biophysica acta.
[6] D. Kleinfeld,et al. Damping of oscillations in the semiquinone absorption in reaction centers after successive flashes determination of the equilibrium between Q(-)AQB and QAQ(-)B. , 1984, Biochimica et biophysica acta.
[7] P. Fromme,et al. Structure of photosystem I. , 2001, Biochimica et biophysica acta.
[8] G. Feher,et al. Electron transfer from the reaction center of Rb. sphaeroides to the quinone pool: Doubly reduced QB leaves the reaction center , 1990 .
[9] B. Rabenstein,et al. Calculation of protonation patterns in proteins with structural relaxation and molecular ensembles – application to the photosynthetic reaction center , 1998, European Biophysics Journal.
[10] H. Michel,et al. The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB. , 1997, Structure.
[11] R. Prince,et al. Electrochemistry of ubiquinones , 1983 .
[12] Tony J. You,et al. Conformation and hydrogen ion titration of proteins: a continuum electrostatic model with conformational flexibility. , 1995, Biophysical journal.
[13] G. Fritzsch,et al. X-ray structure analyses of photosynthetic reaction center variants from Rhodobacter sphaeroides: structural changes induced by point mutations at position L209 modulate electron and proton transfer. , 2001, Biochemistry.
[14] Junjun Mao,et al. How cytochromes with different folds control heme redox potentials. , 2003, Biochemistry.
[15] Robert Eugene Blankenship,et al. Kinetics and thermodynamics of the P870+Q−A → P870+Q−B reaction in isolated reaction centers from the photosynthetic bacterium Rhodopseudomonas sphaeroides , 1984 .
[16] Electrostatic dominoes: long distance propagation of mutational effects in photosynthetic reaction centers of Rhodobacter capsulatus. , 1995, Biochemistry.
[17] E. Alexov,et al. A pragmatic approach to structure based calculation of coupled proton and electron transfer in proteins. , 2000, Biochimica et biophysica acta.
[18] B. Honig,et al. A rapid finite difference algorithm, utilizing successive over‐relaxation to solve the Poisson–Boltzmann equation , 1991 .
[19] G. Feher,et al. Protonation and free energy changes associated with formation of QBH2 in native and Glu-L212-->Gln mutant reaction centers from Rhodobacter sphaeroides. , 1994, Biochemistry.
[20] C. Lancaster. Wolinella succinogenes quinol:fumarate reductase and its comparison to E. coli succinate:quinone reductase , 2003, FEBS letters.
[21] J. Popot,et al. An atypical haem in the cytochrome b6f complex , 2003, Nature.
[22] B. Rabenstein,et al. Energetics of electron-transfer and protonation reactions of the quinones in the photosynthetic reaction center of Rhodopseudomonas viridis. , 1998, Biochemistry.
[23] G. Feher,et al. Pathway of proton transfer in bacterial reaction centers: role of aspartate-L213 in proton transfers associated with reduction of quinoneto dihydroquinone. , 1994, Biochemistry.
[24] M. Schiffer,et al. Temperature and cryoprotectant influence secondary quinone binding position in bacterial reaction centers , 2004, FEBS letters.
[25] P. Beroza,et al. Protonation of interacting residues in a protein by a Monte Carlo method: application to lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[26] D. Lancaster,et al. Ubiquinone reduction and protonation in photosynthetic reaction centres from Rhodopseudomonas viridis: X-ray structures and their functional implications , 1998 .
[27] G. Feher,et al. Proton transfer pathways and mechanism in bacterial reaction centers , 2003, FEBS letters.
[28] M. Gunner,et al. Protons forge new paths. , 2004, Structure.
[29] D. Bendall,et al. A mechanism for the reduction of cytochromes by quinols in solution and its relevance to biological electron transfer reactions , 1979, FEBS letters.
[30] A. Warshel,et al. Electrostatic control of charge separation in bacterial photosynthesis. , 1990, Biochimica et biophysica acta.
[31] S. Sriharan,et al. The fast multipole boundary element method for molecular electrostatics: An optimal approach for large systems , 1995, J. Comput. Chem..
[32] C. Mioskowski,et al. Vibrational spectroscopy favors a unique QB binding site at the proximal position in wild-type reaction centers and in the Pro-L209 --> Tyr mutant from Rhodobacter sphaeroides. , 2002, Biochemistry.
[33] K. Moffat,et al. Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[34] G. Feher,et al. Light-induced proton uptake by photosynthetic reaction centers from Rhodobacter sphaeroides R-26.1. II. Protonation of the state DQAQB2-. , 1993, Biochimica et biophysica acta.
[35] K. Sharp,et al. On the calculation of pKas in proteins , 1993, Proteins.
[36] C. Wraight. Proton and electron transfer in the acceptor quinone complex of photosynthetic reaction centers from Rhodobacter sphaeroides. , 2004, Frontiers in bioscience : a journal and virtual library.
[37] C. Wraight,et al. Investigations on the influence of headgroup substitution and isoprene side-chain length in the function of primary and secondary quinones of bacterial reaction centers. , 1990, Biochimica et biophysica acta.
[38] G. Feher,et al. Observation of the protonated semiquinone intermediate in isolated reaction centers from Rhodobacter sphaeroides: implications for the mechanism of electron and proton transfer in proteins. , 1999, Biochemistry.
[39] E. Alexov,et al. Calculated protein and proton motions coupled to electron transfer: electron transfer from QA- to QB in bacterial photosynthetic reaction centers. , 1999, Biochemistry.
[40] G. Feher,et al. Conformational gating of the electron transfer reaction QA-.QB --> QAQB-. in bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[41] M. Gunner,et al. Backbone dipoles generate positive potentials in all proteins: origins and implications of the effect. , 2000, Biophysical journal.
[42] G. Feher,et al. Identification of the proton pathway in bacterial reaction centers: cooperation between Asp-M17 and Asp-L210 facilitates proton transfer to the secondary quinone (QB). , 2001, Biochemistry.
[43] P. Fyfe,et al. Re-emerging structures: continuing crystallography of the bacterial reaction centre. , 2000, Biochimica et biophysica acta.
[44] S. Walden,et al. Protein Conformational Gate Controlling Binding Site Preference and Migration for Ubiquinone-B in the Photosynthetic Reaction Center of Rhodobacter sphaeroides , 2002 .
[45] Yifan Song,et al. Calculation of proton transfers in Bacteriorhodopsin bR and M intermediates. , 2003, Biochemistry.
[46] E. Alexov,et al. Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties. , 1997, Biophysical journal.
[47] D C Rees,et al. Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. , 1997, Science.
[48] P. Maróti,et al. Conformation-activated protonation in reaction centers of the photosynthetic bacterium Rhodobacter sphaeroides. , 1997, Biochemistry.
[49] C. Lancaster. The role of electrostatics in proton‐conducting membrane protein complexes , 2003, FEBS letters.
[50] J. Breton,et al. Fourier transform infrared evidence of proton uptake by glutamate L212 upon reduction of the secondary quinone QB in the photosynthetic reaction center from Rhodobacter capsulatus. , 2000, Biochemistry.
[51] B. Trumpower,et al. Protonmotive pathways and mechanisms in the cytochrome bc 1 complex , 2003, FEBS letters.
[52] G. Feher,et al. Light-induced proton uptake by photosynthetic reaction centers from Rhodobacter sphaeroides R-26. I. Protonation of the one-electron states D+QA−, DQA−, D+QAQB−, and DQAQB−☆ , 1988 .
[53] D. Kleinfeld,et al. Electron transfer in reaction centers of Rhodopseudomonas sphaeroides. I. Determination of the charge recombination pathway of D+QAQ(-)B and free energy and kinetic relations between Q(-)AQB and QAQ(-)B. , 1984, Biochimica et biophysica acta.
[54] B. Diner,et al. Effect of inhibitors, redox state and isoprenoid chain length on the affinity of ubiquinone for the secondary acceptor binding site in the reaction centers of photosynthetic bacteria , 1984 .
[55] P. Faller,et al. The heart of photosynthesis in glorious 3D. , 2001, Trends in biochemical sciences.
[56] M. Gunner,et al. Trapping conformational intermediate states in the reaction center protein from photosynthetic bacteria. , 2001, Biochemistry.
[57] M. Schiffer,et al. Long-range electrostatic interaction in the bacterial photosynthetic reaction centre , 1995, Nature Structural Biology.
[58] B. Trumpower. Function of quinones in energy conserving systems , 1982 .
[59] Janet L. Smith,et al. Evolution of photosynthesis: time-independent structure of the cytochrome b6f complex. , 2004, Biochemistry.
[60] T. Simonson,et al. Macromolecular electrostatics: continuum models and their growing pains. , 2001, Current opinion in structural biology.
[61] B. Rabenstein,et al. Electron transfer between the quinones in the photosynthetic reaction center and its coupling to conformational changes. , 2000, Biochemistry.
[62] K. Sharp,et al. Accurate Calculation of Hydration Free Energies Using Macroscopic Solvent Models , 1994 .
[63] P. Dutton,et al. Influence of QA site redox cofactor structure on equilibrium binding, in situ electrochemistry, and electron-transfer performance in the photosynthetic reaction center protein. , 1993, Biochemistry.
[64] P. Dutton,et al. Direct measurement of the midpoint potential of the primary electron acceptor in Rhodopseudomonas spheroides in situ and in the isolated state: Some relationships with pH and o‐phenanthroline , 1973, FEBS letters.
[65] C. Wraight. Electron acceptors of bacterial photosynthetic reaction centers. II. H+ binding coupled to secondary electron transfer in the quinone acceptor complex. , 1979, Biochimica et biophysica acta.
[66] J. Lavergne,et al. Interactions between the donor and acceptor sides in bacterial reaction centers. , 2000, Biochemistry.
[67] G. Feher,et al. Pathway of proton transfer in bacterial reaction centers: second-site mutation Asn-M44-->Asp restores electron and proton transfer in reaction centers from the photosynthetically deficient Asp-L213-->Asn mutant of Rhodobacter sphaeroides. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[68] E. Alexov,et al. Modeling the effects of mutations on the free energy of the first electron transfer from QA- to QB in photosynthetic reaction centers. , 2000, Biochemistry.
[69] G. Feher,et al. X-Ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides; altered proton transfer pathways. , 2004, Structure.
[70] J. Lavergne,et al. Electron and proton transfer on the acceptor side of the reaction center in chromatophores of Rhodobacter capsulatus: evidence for direct protonation of the semiquinone state of QB. , 1999, Biochemistry.
[71] Jeremy C. Smith,et al. The position of QB in the photosynthetic reaction center depends on pH: a theoretical analysis of the proton uptake upon QB reduction. , 2003, Biophysical journal.
[72] M. Okamura,et al. Rapid-scan Fourier transform infrared spectroscopy shows coupling of GLu-L212 protonation and electron transfer to Q(B) in Rhodobacter sphaeroides reaction centers. , 2002, Biochimica et biophysica acta.
[73] David A. Case,et al. Including Side Chain Flexibility in Continuum Electrostatic Calculations of Protein Titration , 1996 .
[74] Barry Honig,et al. Extending the Applicability of the Nonlinear Poisson−Boltzmann Equation: Multiple Dielectric Constants and Multivalent Ions† , 2001 .
[75] P. Beroza,et al. Electrostatic calculations of amino acid titration and electron transfer, Q-AQB-->QAQ-B, in the reaction center. , 1995, Biophysical journal.
[76] G. Feher,et al. Mechanism of Proton-Coupled Electron Transfer for Quinone (QB) Reduction in Reaction Centers of Rb. Sphaeroides , 1996 .
[77] P. Dutton,et al. Kinetic studies on the reaction center protein from Rhodopseudomonas sphaeroides: the temperature and free energy dependence of electron transfer between various quinones in the QA site and the oxidized bacteriochlorophyll dimer , 1986 .
[78] G. Feher,et al. Identification of the proton pathway in bacterial reaction centers: inhibition of proton transfer by binding of Zn2+ or Cd2+. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[79] G. Gordillo,et al. The electrochemistry of ubiquinone-10 in a phospholipid model membrane. , 2000, Faraday discussions.
[80] D. Kleinfeld,et al. Electron transfer in reaction centers of Rhodopseudomonas sphaeroides. II. Free energy and kinetic relations between the acceptor states Q(-)A Q(-)B and QAQ(2-)B. , 1985, Biochimica et biophysica acta.
[81] A. Rutherford,et al. Direct measurement of the redox potential of the primary and secondary quinone electron acceptors in Rhodopseudomonas sphaeroides (wild‐type) by EPR Spectrometry , 1980, FEBS letters.
[82] G. Feher,et al. Pathway of proton transfer in bacterial reaction centers: replacement of serine-L223 by alanine inhibits electron and proton transfers associated with reduction of quinone to dihydroquinone. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[83] W. W. Parson,et al. Temperature and detection-wavelength dependence of the picosecond electron-transfer kinetics measured in Rhodopseudomonas sphaeroides reaction centers. Resolution of new spectral and kinetic components in the primary charge-separation process , 1985 .
[84] E. Alexov,et al. Combining conformational flexibility and continuum electrostatics for calculating pK(a)s in proteins. , 2002, Biophysical journal.
[85] G. Feher,et al. Pathway of proton transfer in bacterial reaction centers: replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[86] Anthony K. Grafton,et al. AMINO ACID PROTONATION STATES DETERMINE BINDING SITES OF THE SECONDARY UBIQUINONE AND ITS ANION IN THE RHODOBACTER SPHAEROIDES PHOTOSYNTHETIC REACTION CENTER , 1999 .
[87] M. Gunner,et al. -deltaG(AB) and pH dependence of the electron transfer from P(+)Q(A)(-)Q(B) toP(+)Q(A)Q(B)(-) in Rhodobacter sphaeroides reaction centers. , 2000, Biochemistry.
[88] Klaus Gerwert,et al. Coupling of light-induced electron transfer to proton uptake in photosynthesis , 2003, Nature Structural Biology.
[89] B. Honig,et al. Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopseudomonas viridis. , 1996, Biophysical journal.
[90] E. Knapp,et al. Redox potential of quinones in photosynthetic reaction centers from Rhodobacter sphaeroides: dependence on protonation of Glu-L212 and Asp-L213. , 2003, Biochemistry.
[91] M. Gunner,et al. Kinetic phases in the electron transfer from P+QA-QB to P+QAQB- and the associated processes in Rhodobacter sphaeroides R-26 reaction centers. , 1998, Biochemistry.
[92] E. Takahashi,et al. Proton and electron transfer in the acceptor quinone complex of Rhodobacter sphaeroides reaction centers: characterization of site-directed mutants of the two ionizable residues, GluL212 and AspL213, in the QB binding site. , 1992, Biochemistry.
[93] Wilfred F. van Gunsteren,et al. Computation of free energy , 2002 .
[94] Genji Kurisu,et al. Structure of the Cytochrome b6f Complex of Oxygenic Photosynthesis: Tuning the Cavity , 2003, Science.
[95] M. Okamura,et al. Simultaneous replacement of Asp-L210 and Asp-M17 with Asn increases proton uptake by Glu-L212 upon first electron transfer to QB in reaction centers from Rhodobacter sphaeroides. , 2001, Biochemistry.
[96] A. Warshel,et al. What are the dielectric “constants” of proteins and how to validate electrostatic models? , 2001, Proteins.
[97] B. Honig,et al. Calculation of the total electrostatic energy of a macromolecular system: Solvation energies, binding energies, and conformational analysis , 1988, Proteins.
[98] G. Fritzsch,et al. Charge separation induces conformational changes in the photosynthetic reaction centre of purple bacteria. , 2002, Acta crystallographica. Section D, Biological crystallography.
[99] C. A. Bishop,et al. Equilibria of Substituted Semiquinones at High pH , 1965 .
[100] G. Fritzsch,et al. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: cofactors and protein-cofactor interactions. , 1994, Structure.
[101] A. Cámara-Artigas,et al. Interactions between lipids and bacterial reaction centers determined by protein crystallography , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[102] P. Dutton,et al. Experimental resolution of the free energies of aqueous solvation contributions to ligand-protein binding: quinone-QA site interactions in the photosynthetic reaction center protein. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[103] B. Honig,et al. ELECTROSTATIC POTENTIALS IN RHODOPSEUDOMONAS VIRIDIS REACTION CENTERS : IMPLICATIONS FOR THE DRIVING FORCE AND DIRECTIONALITY OF ELECTRON TRANSFER , 1996 .
[104] P. Rich. The quinone chemistry of bc complexes. , 2004, Biochimica et biophysica acta.