메뉴 건너뛰기




Volumn 84, Issue 3, 2003, Pages 2090-2098

The position of QB in the photosynthetic reaction center depends on pH: A theoretical analysis of the proton uptake upon QB reduction

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHEOPHYTIN; NONHEME IRON PROTEIN;

EID: 0037342175     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)75016-4     Document Type: Article
Times cited : (30)

References (70)
  • 1
    • 0031708266 scopus 로고    scopus 로고
    • Electrostatics and the ion selectivity of ligand-gated channels
    • Adcock, C., G. Smith, and M. Sansom. 1998. Electrostatics and the ion selectivity of ligand-gated channels. Biophys. J. 75:1211-1222.
    • (1998) Biophys. J. , vol.75 , pp. 1211-1222
    • Adcock, C.1    Smith, G.2    Sansom, M.3
  • 4
    • 0033614791 scopus 로고    scopus 로고
    • B in bacterial photosynthetic reaction centers
    • B in bacterial photosynthetic reaction centers. Biochemistry. 38:8253-8270.
    • (1999) Biochemistry , vol.38 , pp. 8253-8270
    • Alexov, E.G.1    Gunner, M.R.2
  • 5
    • 0027973329 scopus 로고
    • Crystallization of the reaction center from Rhodobacter sphaeroides in a new tetragonal form
    • Allen, J. 1994. Crystallization of the reaction center from Rhodobacter sphaeroides in a new tetragonal form. Proteins. 20:283-286.
    • (1994) Proteins , vol.20 , pp. 283-286
    • Allen, J.1
  • 7
    • 0035120969 scopus 로고    scopus 로고
    • Some theoretical and computational aspects of the inclusion of proton isomerism in the protonation equilibrium of proteins
    • Baptista, A., and C. Soares. 2001. Some Theoretical and Computational Aspects of the Inclusion of Proton Isomerism in the Protonation Equilibrium of Proteins. J. Phys. Chem. B. 105:293-309.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 293-309
    • Baptista, A.1    Soares, C.2
  • 9
    • 0026612756 scopus 로고
    • a values of ionizable groups in bacteriorhodopsin
    • a values of ionizable groups in bacteriorhodopsin. J. Mol. Biol. 224:473-486.
    • (1992) J. Mol. Biol. , vol.224 , pp. 473-486
    • Bashford, D.1    Gerwert, K.2
  • 10
    • 0025197061 scopus 로고
    • a's of ionizable groups in proteins: Atomic detail from a continuum electrostatic model
    • a's of ionizable groups in proteins: atomic detail from a continuum electrostatic model. Biochemistry. 29:10219-10225.
    • (1990) Biochemistry , vol.29 , pp. 10219-10225
    • Bashford, D.1    Karplus, M.2
  • 11
    • 0032319206 scopus 로고    scopus 로고
    • Calculations of proton-binding thermodynamics in proteins
    • Beroza, P., and D. A. Case. 1998. Calculations of proton-binding thermodynamics in proteins. Methods Enzymol. 295:170-189.
    • (1998) Methods Enzymol. , vol.295 , pp. 170-189
    • Beroza, P.1    Case, D.A.2
  • 12
    • 0026095641 scopus 로고
    • Protonation of interacting residues in a protein by a Monte Carlo method: Application to lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides
    • Beroza, P., D. R. Fredkin, M. Y. Okamura, and G. Feher. 1991. Protonation of interacting residues in a protein by a Monte Carlo method: application to lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides. Proc. Natl. Acad. Sci. USA. 88:5804-5808.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5804-5808
    • Beroza, P.1    Fredkin, D.R.2    Okamura, M.Y.3    Feher, G.4
  • 15
    • 0024250301 scopus 로고
    • Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparison
    • Brunger, A. T., and M. Karplus. 1988. Polar hydrogen positions in proteins: empirical energy placement and neutron diffraction comparison. Proteins. 4:148-156.
    • (1988) Proteins , vol.4 , pp. 148-156
    • Brunger, A.T.1    Karplus, M.2
  • 16
    • 0000878023 scopus 로고
    • - in bacterial reaction centers: Measurement of light-induced electrogenic events in RCs incorporated in a phospholipid bilayer
    • J. B. A. Vermeglio, editor. Plenum Press, New York
    • - in Bacterial Reaction centers: Measurement of Light-Induced Electrogenic Events in RCs Incorporated in a Phospholipid Bilayer. In: The Photosynthetic Bacterial Reaction Center II. J. B. A. Vermeglio, editor. Plenum Press, New York. 321-330
    • (1992) The Photosynthetic Bacterial Reaction Center II , pp. 321-330
    • Brzezinski, P.1    Okamura, M.Y.2    Feher, G.3
  • 17
    • 0025784505 scopus 로고
    • Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides
    • Chang, C., O. el-Kabbani, D. Tiede, J. Norris, and M. Schiffer. 1991. Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry. 30:5352-5360.
    • (1991) Biochemistry , vol.30 , pp. 5352-5360
    • Chang, C.1    El-Kabbani, O.2    Tiede, D.3    Norris, J.4    Schiffer, M.5
  • 18
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3Å resolution
    • Deisenhofer, J., O. Epp, K. Miki, R. Huber, and H. Michel. 1985. Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3Å resolution. Nature. 318:618-624.
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 19
    • 0005384356 scopus 로고
    • Nobel lecture. The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis
    • Deisenhofer, J., and H. Michel. 1989. Nobel lecture. The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis. EMBO J. 8:2149-2170.
    • (1989) EMBO J. , vol.8 , pp. 2149-2170
    • Deisenhofer, J.1    Michel, H.2
  • 20
    • 0028774335 scopus 로고
    • Structure of the Photosynthetic Reaction Centre from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactors and protein-cofactor interactions
    • Ermler, U., G. Fritzsch, S. K. Buchanan, and H. Michel. 1994. Structure of the Photosynthetic Reaction Centre from Rhodobacter sphaeroides at 2.65 Å resolution: cofactors and protein-cofactor interactions. Structure. 2:925-936.
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 21
    • 85031206620 scopus 로고    scopus 로고
    • 2+ binding effect on bacterial reaction center mutants: The proton penetration involves interdependent pathways
    • Abstr.
    • 2+ binding effect on bacterial reaction center mutants: the proton penetration involves interdependent pathways. Biophys. J. 80:518a. (Abstr.)
    • (2002) Biophys. J. , vol.80
    • Gerencser, L.1    Taly, A.2    Baciou, L.3    Maroti, P.4    Sebban, P.5
  • 23
    • 0001178664 scopus 로고    scopus 로고
    • Amino acid protonation states determine binding sites of the secondary ubiquinone and its anion in the Rhodobacter sphaeroides photosynthetic reaction center
    • Grafton, A. K., and R. A. Wheeler. 1999. Amino acid protonation states determine binding sites of the secondary ubiquinone and its anion in the Rhodobacter sphaeroides photosynthetic reaction center. J. Phys. Chem. B. 103:5380-5387.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 5380-5387
    • Grafton, A.K.1    Wheeler, R.A.2
  • 24
    • 0032578541 scopus 로고    scopus 로고
    • -. In bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay
    • -. in bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay. Proc. Natl. Acad. Sci. USA. 95:11679-11684.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11679-11684
    • Graige, M.S.1    Feher, G.2    Okamura, M.Y.3
  • 25
    • 0034640465 scopus 로고    scopus 로고
    • A pragmatic approach to structure based calculation of coupled proton and electron transfer in proteins
    • Gunner, M. R., and E. Alexov. 2000. A pragmatic approach to structure based calculation of coupled proton and electron transfer in proteins. Biochim. Biophys. Acta. 1458:63-87.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 63-87
    • Gunner, M.R.1    Alexov, E.2
  • 26
    • 0344187406 scopus 로고
    • Gated electron transfer: When are observed rates controlled by conformational interconversion?
    • Hoffman, B. M., and M. A. Ratner. 1987. Gated electron transfer: when are observed rates controlled by conformational interconversion? J. Am. Chem. Soc. 109:6237-6243.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 6237-6243
    • Hoffman, B.M.1    Ratner, M.A.2
  • 27
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig, B., and A. Nicholls. 1995. Classical electrostatics in biology and chemistry. Science. 268:1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 29
    • 0036151820 scopus 로고    scopus 로고
    • Protonation and stability of the globular domain of influenza virus hemagglutinin
    • Huang, Q., R. Opitz, E. W. Knapp, and A. Herrmann. 2002. Protonation and stability of the globular domain of influenza virus hemagglutinin. Biophys. J. 82:1050-1058.
    • (2002) Biophys. J. , vol.82 , pp. 1050-1058
    • Huang, Q.1    Opitz, R.2    Knapp, E.W.3    Herrmann, A.4
  • 30
    • 0022964504 scopus 로고
    • Focusing of electric fields in the active site of Cu-Zn superoxide dismutase: Effects of ionic strength and amino-acid modification
    • Klapper, I., R. Fine, K. A. Sharp, and B. H. Honig. 1986. Focusing of electric fields in the active site of Cu-Zn superoxide dismutase: effects of ionic strength and amino-acid modification. Proteins. 1:47-59.
    • (1986) Proteins , vol.1 , pp. 47-59
    • Klapper, I.1    Fine, R.2    Sharp, K.A.3    Honig, B.H.4
  • 31
    • 0035836485 scopus 로고    scopus 로고
    • 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
    • Kuglstatter, A., U. Ermler, H. Michel, L. Baciou, and G. Fritzsch. 2001. 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. Biochemistry. 40:4253-4260.
    • (2001) Biochemistry , vol.40 , pp. 4253-4260
    • Kuglstatter, A.1    Ermler, U.2    Michel, H.3    Baciou, L.4    Fritzsch, G.5
  • 32
    • 0032877515 scopus 로고    scopus 로고
    • Quinone-binding sites in membrane proteins: What can we learn from the Rhodopseudomonas viridis reaction centre?
    • Lancaster, C. R. 1999a. Quinone-binding sites in membrane proteins: what can we learn from the Rhodopseudomonas viridis reaction centre? Biochem. Soc. Trans. 27:591-596.
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 591-596
    • Lancaster, C.R.1
  • 33
    • 0034671487 scopus 로고    scopus 로고
    • Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-A resolution
    • Lancaster, C. R., M. V. Bibikova, P. Sabatino, D. Oesterhelt, and H. Michel. 2000. Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-A resolution. J. Biol. Chem. 275:39364-39368.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39364-39368
    • Lancaster, C.R.1    Bibikova, M.V.2    Sabatino, P.3    Oesterhelt, D.4    Michel, H.5
  • 35
    • 0030030176 scopus 로고    scopus 로고
    • Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopseudomonas viridis
    • Lancaster, C. R., H. Michel, B. Honig, and M. R. Gunner. 1996. Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopseudomonas viridis. Biophys. J. 70:2469-2492.
    • (1996) Biophys. J. , vol.70 , pp. 2469-2492
    • Lancaster, C.R.1    Michel, H.2    Honig, B.3    Gunner, M.R.4
  • 36
    • 0000706753 scopus 로고    scopus 로고
    • The structure of the Rhodopseudomonas viridis reaction centre - An overview and recent advances
    • G. Garab, Editor, Kluwer, Dordrecht, NL
    • Lancaster, C. R. D. 1999b. The structure of the Rhodopseudomonas viridis reaction centre - an overview and recent advances. In Photosynthesis: Mechanisms and Effects. Vol 2. G. Garab, Editor, Kluwer, Dordrecht, NL. 673-678
    • (1999) Photosynthesis: Mechanisms and Effects , vol.2 , pp. 673-678
    • Lancaster, C.R.D.1
  • 37
    • 0032478280 scopus 로고    scopus 로고
    • - and the associated processes in Rhodobacter sphaeroides R-26 reaction centers
    • - and the associated processes in Rhodobacter sphaeroides R-26 reaction centers. Biochemistry. 37:2818-2829.
    • (1998) Biochemistry , vol.37 , pp. 2818-2829
    • Li, J.1    Gilroy, D.2    Tiede, D.M.3    Gunner, M.R.4
  • 38
    • 85031202268 scopus 로고    scopus 로고
    • Kinetics and energetics of photocycle in reaction center of photosynthetic bacteria
    • Maróti, P., and S. Osváth. 1997. Kinetics and energetics of photocycle in reaction center of photosynthetic bacteria. Eur. Biophys. J. 26:103.
    • (1997) Eur. Biophys. J. , vol.26 , pp. 103
    • Maróti, P.1    Osváth, S.2
  • 39
    • 0001334882 scopus 로고
    • + binding by bacterial photosynthetic reaction centers: Influences of the redox states of the acceptor quinones and primary donor
    • + binding by bacterial photosynthetic reaction centers: influences of the redox states of the acceptor quinones and primary donor. Biochim. Biophys. Acta. 934:329-347.
    • (1988) Biochim. Biophys. Acta , vol.934 , pp. 329-347
    • Maroti, P.1    Wraight, C.A.2
  • 40
    • 0034642179 scopus 로고    scopus 로고
    • Ubiquinone binding, ubiquinone exclusion, and detailed cofactor conformation in a mutant bacterial reaction center
    • McAuley, K. E., P. K. Fyfe, J. P. Ridge, R. J. Cogdell, N. W. Isaacs, and M. R. Jones. 2000. Ubiquinone binding, ubiquinone exclusion, and detailed cofactor conformation in a mutant bacterial reaction center. Biochemistry. 39:15032-15043.
    • (2000) Biochemistry , vol.39 , pp. 15032-15043
    • McAuley, K.E.1    Fyfe, P.K.2    Ridge, J.P.3    Cogdell, R.J.4    Isaacs, N.W.5    Jones, M.R.6
  • 43
    • 0033461176 scopus 로고    scopus 로고
    • Conformationally controlled pK-switching in membrane proteins: One more mechanism specific to the enzyme catalysis?
    • Mulkidjanian, A. Y. 1999. Conformationally controlled pK-switching in membrane proteins: one more mechanism specific to the enzyme catalysis? FEBS Lett. 463:199-204.
    • (1999) FEBS Lett. , vol.463 , pp. 199-204
    • Mulkidjanian, A.Y.1
  • 44
    • 0028973591 scopus 로고
    • Fourier transforms infrared difference spectroscopy of secondary quinone acceptor photoreduction in proton transfer mutants of Rhodobacter sphaeroides
    • Nabedryk, E., J. Breton, R. Hienerwadel, C. Fogel, W. Mäntele, M. L. Paddock, and M. Y. Okamura. 1995. Fourier transforms infrared difference spectroscopy of secondary quinone acceptor photoreduction in proton transfer mutants of Rhodobacter sphaeroides. Biochemistry. 34:14722-14732.
    • (1995) Biochemistry , vol.34 , pp. 14722-14732
    • Nabedryk, E.1    Breton, J.2    Hienerwadel, R.3    Fogel, C.4    Mäntele, W.5    Paddock, M.L.6    Okamura, M.Y.7
  • 46
    • 0035957234 scopus 로고    scopus 로고
    • A novel view of pH titration in biomolecules
    • Onufriev, A., D. A. Case, and G. M. Ullmann. 2001. A novel view of pH titration in biomolecules. Biochemistry. 40:3413-3419.
    • (2001) Biochemistry , vol.40 , pp. 3413-3419
    • Onufriev, A.1    Case, D.A.2    Ullmann, G.M.3
  • 48
    • 0035112206 scopus 로고    scopus 로고
    • Calculated pH-dependent population and protonation of carbon-monoxy-myoglobin conformers
    • Rabenstein, B., and E. W. Knapp. 2001. Calculated pH-dependent population and protonation of carbon-monoxy-myoglobin conformers. Biophys. J. 80:1141-1150.
    • (2001) Biophys. J. , vol.80 , pp. 1141-1150
    • Rabenstein, B.1    Knapp, E.W.2
  • 49
    • 0032562210 scopus 로고    scopus 로고
    • Energetics of electron-transfer and protonation reactions of the quinones in the photosynthetic reaction center of Rhodopseudomonas viridis
    • Rabenstein, B., G. M. Ullmann, and E. W. Knapp. 1998. Energetics of electron-transfer and protonation reactions of the quinones in the photosynthetic reaction center of Rhodopseudomonas viridis. Biochemistry. 37:2488-2495.
    • (1998) Biochemistry , vol.37 , pp. 2488-2495
    • Rabenstein, B.1    Ullmann, G.M.2    Knapp, E.W.3
  • 50
    • 0034730115 scopus 로고    scopus 로고
    • Electron transfer between the quinones in the photosynthetic reaction center and its coupling to conformational changes
    • Rabenstein, B., G. M. Ullmann, and E. W. Knapp. 2000. Electron transfer between the quinones in the photosynthetic reaction center and its coupling to conformational changes. Biochemistry. 39:10487-10496.
    • (2000) Biochemistry , vol.39 , pp. 10487-10496
    • Rabenstein, B.1    Ullmann, G.M.2    Knapp, E.W.3
  • 51
    • 0028787627 scopus 로고
    • Electron and proton transfer to the quinones in bacterial photosynthetic reaction centers: Insight from combined approaches of molecular genetics and biophysics
    • published erratum appears in Biochimie. 1995. 77:after table of contents
    • Sebban, P., P. Maróti, and D. K. Hanson. 1995a. Electron and proton transfer to the quinones in bacterial photosynthetic reaction centers: insight from combined approaches of molecular genetics and biophysics. Biochimie. 77:677-694 [published erratum appears in Biochimie. 1995. 77:after table of contents].
    • (1995) Biochimie , vol.77 , pp. 677-694
    • Sebban, P.1    Maróti, P.2    Hanson, D.K.3
  • 52
    • 0029007257 scopus 로고
    • Electrostatic dominoes: Long distance propagation of mutational effects in photosynthetic reaction centers of Rhodobacter capsulatus
    • Sebban, P., P. Maróti, M. Schiffer, and D. K. Hanson. 1995b. Electrostatic dominoes: long distance propagation of mutational effects in photosynthetic reaction centers of Rhodobacter capsulatus. Biochemistry. 34:8390-8397.
    • (1995) Biochemistry , vol.34 , pp. 8390-8397
    • Sebban, P.1    Maróti, P.2    Schiffer, M.3    Hanson, D.K.4
  • 53
    • 0029038105 scopus 로고
    • Salt effects on polyelectrolyte-ligand binding: Comparison of Poisson-Boltzmann, and limiting law/counterion binding models
    • Sharp, K. A., R. A. Friedman, V. Misra, J. Hecht, and B. Honig. 1995. Salt effects on polyelectrolyte-ligand binding: comparison of Poisson-Boltzmann, and limiting law/counterion binding models. Biopolymers. 36:245-262.
    • (1995) Biopolymers , vol.36 , pp. 245-262
    • Sharp, K.A.1    Friedman, R.A.2    Misra, V.3    Hecht, J.4    Honig, B.5
  • 54
    • 0025283002 scopus 로고
    • Electrostatic interactions in macro-molecules: Theory and applications
    • Sharp, K. A., and B. Honig. 1990. Electrostatic interactions in macro-molecules: theory and applications. Annu. Rev. Biophys. Biophys. Chem. 19:301-332.
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 301-332
    • Sharp, K.A.1    Honig, B.2
  • 55
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron-proton transfer
    • Stowell, M. H., T. M. McPhillips, D. C. Rees, S. M. Soltis, E. Abresch, and G. Feher. 1997. Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Science. 276:812-816.
    • (1997) Science , vol.276 , pp. 812-816
    • Stowell, M.H.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 56
    • 33947488796 scopus 로고
    • Nuclear magnetic resonance studies of protonation of polyamine and aminocarboxylate compounds in aqueous solution
    • Sudmeier, J. L., and C. N. Reilley. 1964. Nuclear Magnetic Resonance Studies of Protonation of Polyamine and Aminocarboxylate Compounds in Aqueous Solution. Anal. Chem. 36:1698-1706.
    • (1964) Anal. Chem. , vol.36 , pp. 1698-1706
    • Sudmeier, J.L.1    Reilley, C.N.2
  • 58
    • 0015520587 scopus 로고
    • Interpretation of protein titration curves. Application to lysozyme
    • Tanford, C., and R. Roxby. 1972. Interpretation of protein titration curves. Application to lysozyme. Biochemistry. 11:2192-2198.
    • (1972) Biochemistry , vol.11 , pp. 2192-2198
    • Tanford, C.1    Roxby, R.2
  • 59
    • 0036359052 scopus 로고    scopus 로고
    • Studies of the reduction and protonation behavior of tetraheme cytochromes using atomic detail
    • Teixeira, V., C. Soares, and A. Baptista. 2002. Studies of the reduction and protonation behavior of tetraheme cytochromes using atomic detail. J. Biol. Inorg. Chem. 7:200-216.
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 200-216
    • Teixeira, V.1    Soares, C.2    Baptista, A.3
  • 61
    • 0029769668 scopus 로고    scopus 로고
    • Time-resolved electrochromism associated with the formation of quinone anions in the Rhodobacter sphaeroides R26 reaction center
    • Tiede, D. M., J. Vazquez, J. Cordova, and P. A. Marone. 1996. Time-resolved electrochromism associated with the formation of quinone anions in the Rhodobacter sphaeroides R26 reaction center. Biochemistry. 35:10763-10775.
    • (1996) Biochemistry , vol.35 , pp. 10763-10775
    • Tiede, D.M.1    Vazquez, J.2    Cordova, J.3    Marone, P.A.4
  • 63
    • 0000000699 scopus 로고    scopus 로고
    • Electrostatic models for computing protonation and redox equilibria in proteins
    • Ullmann, G. M., and E. W. Knapp. 1999. Electrostatic models for computing protonation and redox equilibria in proteins. Eur. Biophys. J. 28:533-551.
    • (1999) Eur. Biophys. J. , vol.28 , pp. 533-551
    • Ullmann, G.M.1    Knapp, E.W.2
  • 64
    • 0031041540 scopus 로고    scopus 로고
    • Computational simulation and analysis of the dynamic association between plastocyanin and cytochrome f. Consequences for the electron-transfer reaction
    • Ullmann, G. M., E. W. Knapp, and N. M. Kostic. 1997. Computational Simulation and Analysis of the Dynamic Association between Plastocyanin and Cytochrome f. Consequences for the Electron-transfer Reaction. J. Am. Chem. Soc. 119:42-52.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 42-52
    • Ullmann, G.M.1    Knapp, E.W.2    Kostic, N.M.3
  • 65
    • 0037149804 scopus 로고    scopus 로고
    • Protein conformational gate controlling binding site preference and migration for ubiquinone-B in the photosynthetic reaction center of Rhodobacter sphaeroides
    • Walden, S. E., and R. A. Wheeler. 2002. Protein Conformational Gate Controlling Binding Site Preference and Migration for Ubiquinone-B in the Photosynthetic Reaction Center of Rhodobacter sphaeroides. J. Phys. Chem. B. 106:3001-3006.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 3001-3006
    • Walden, S.E.1    Wheeler, R.A.2
  • 66
    • 0018785093 scopus 로고
    • + binding coupled to secondary electron transfer in the quinone acceptor complex
    • + binding coupled to secondary electron transfer in the quinone acceptor complex. Biochim. Biophys. Acta. 548:309-327.
    • (1979) Biochim. Biophys. Acta , vol.548 , pp. 309-327
    • Wraight, C.A.1
  • 68
    • 0035371680 scopus 로고    scopus 로고
    • B in Rhodopseudomonas viridis photosynthetic reaction centers
    • B in Rhodopseudomonas viridis photosynthetic reaction centers. Biochim. Biophys. Acta. 1505:280-290.
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 280-290
    • Zachariae, U.1    Lancaster, C.R.2
  • 69
    • 0000253530 scopus 로고
    • Gating of photoinduced electron transfer from zinc cytochrome c and tin cytochrome c to plastocyanin. Effects of solution viscosity on rearrangement of the metalloprotein complex
    • Zhou, J. S., and N. M. Kostic. 1993. Gating of photoinduced electron transfer from zinc cytochrome c and tin cytochrome c to plastocyanin. Effects of solution viscosity on rearrangement of the metalloprotein complex. J. Am. Chem. Soc. 115:10796-10804.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 10796-10804
    • Zhou, J.S.1    Kostic, N.M.2
  • 70
    • 0018790743 scopus 로고
    • The influence of electrostatic interaction on the proton-binding behaviour of myoinositol hexakisphosphate
    • Zuiderweg, E. R., G. G. van Beek, and S. H. de Bruin. 1979. The influence of electrostatic interaction on the proton-binding behaviour of myoinositol hexakisphosphate. Eur. J. Biochem. 94:297-306.
    • (1979) Eur. J. Biochem. , vol.94 , pp. 297-306
    • Zuiderweg, E.R.1    Van Beek, G.G.2    De Bruin, S.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.