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Volumn 97, Issue 1, 2008, Pages 33-53

Investigating the mechanisms of photosynthetic proteins using continuum electrostatics

Author keywords

Docking; Electrostatic potential; Master equation; Membrane potential; pH and redox titration; Poisson Boltzmann equation; Spectral tuning

Indexed keywords

PROTEIN;

EID: 48449102215     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-008-9306-1     Document Type: Review
Times cited : (16)

References (145)
  • 2
    • 0035807787 scopus 로고    scopus 로고
    • Identification of the proton pathway in bacterial reaction centers: Decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors
    • P Ädelroth ML Paddock A Tehrani JT Beatty G Feher M Okamura 2001 Identification of the proton pathway in bacterial reaction centers: decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors Biochemistry 40 14538 14546
    • (2001) Biochemistry , vol.40 , pp. 14538-14546
    • Ädelroth, P.1    Paddock, M.L.2    Tehrani, A.3    Beatty, J.T.4    Feher, G.5    Okamura, M.6
  • 3
    • 33749521844 scopus 로고    scopus 로고
    • How proteins trigger excitation energy transfer in the FMO complex of green sulfur bacteria
    • J Adolphs T Renger 2006 How proteins trigger excitation energy transfer in the FMO complex of green sulfur bacteria Biophys J 91 2778
    • (2006) Biophys J , vol.91 , pp. 2778
    • Adolphs, J.1    Renger, T.2
  • 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
  • 10
    • 84957665033 scopus 로고    scopus 로고
    • An object-oriented programming suite for electrostatic effects in biological molecules
    • Ishikawa Y, Oldehoeft RR, Reynders JVW, Tholburn M (eds) Springer
    • Bashford D (1997) An object-oriented programming suite for electrostatic effects in biological molecules. In: Ishikawa Y, Oldehoeft RR, Reynders JVW, Tholburn M (eds) Scientific computing in object-oriented parallel environments. Springer, pp 233-240
    • (1997) Scientific Computing in Object-oriented Parallel Environments , pp. 233-240
    • Bashford, D.1
  • 11
    • 0025197061 scopus 로고
    • as of ionizable groups in proteins: Atomic detail from a continuum electrostatic model
    • as 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
  • 12
    • 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
  • 13
    • 34047216797 scopus 로고    scopus 로고
    • Simulation of the electron transfer between the tetraheme-subunit and the special pair of the photosynthetic reaction center using a microstate description
    • T Becker RT Ullmann GM Ullmann 2007 Simulation of the electron transfer between the tetraheme-subunit and the special pair of the photosynthetic reaction center using a microstate description J Phys Chem B 111 2957 2968
    • (2007) J Phys Chem B , vol.111 , pp. 2957-2968
    • Becker, T.1    Ullmann, R.T.2    Ullmann, G.M.3
  • 14
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 Å resolution
    • H Belrhali P Nollert A Royant C Menzel JP Rosenbusch EM Landau E Pebay-Peyroula 1999 Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution Structure 7 909 917
    • (1999) Structure , vol.7 , pp. 909-917
    • Belrhali, H.1    Nollert, P.2    Royant, A.3    Menzel, C.4    Rosenbusch, J.P.5    Landau, E.M.6    Pebay-Peyroula, E.7
  • 15
    • 7744224151 scopus 로고
    • Electron-tunneling pathways in ruthenated proteins: Influences on transfer rate
    • DN Beratan JN Onuchic 1989 Electron-tunneling pathways in ruthenated proteins: influences on transfer rate Photosynth Res 22 173 186
    • (1989) Photosynth Res , vol.22 , pp. 173-186
    • Beratan, D.N.1    Onuchic, J.N.2
  • 16
    • 0039359652 scopus 로고
    • Limiting forms of the tunneling matrix element in the long distance bridged electron transfer problem
    • DN Beratan JN Onuchic JJ Hopfield 1985 Limiting forms of the tunneling matrix element in the long distance bridged electron transfer problem J Chem Phys 83 5325 5329
    • (1985) J Chem Phys , vol.83 , pp. 5325-5329
    • Beratan, D.N.1    Onuchic, J.N.2    Hopfield, J.J.3
  • 18
    • 0026434593 scopus 로고
    • Protein electron transfer rates set by the briding secondary and tertiary structure
    • DN Beratan JN Betts JN Onuchic 1991 Protein electron transfer rates set by the briding secondary and tertiary structure Science 252 1285 1288
    • (1991) Science , vol.252 , pp. 1285-1288
    • Beratan, D.N.1    Betts, J.N.2    Onuchic, J.N.3
  • 19
    • 0026095641 scopus 로고
    • Protonation of interacting residues in a protein by a Monte Carlo method: Application to lysozyme and the photosynthetic reaction center
    • P Beroza DR Fredkin MY Okamura G Feher 1991 Protonation of interacting residues in a protein by a Monte Carlo method: application to lysozyme and the photosynthetic reaction center 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
  • 20
    • 0003058940 scopus 로고
    • Mapping electron tunneling pathways: An algorithm that finds the "minimum length"/maximum coupling pathway between electron donors and acceptors in proteins
    • JN Betts DN Beratan JN Onuchic 1992 Mapping electron tunneling pathways: an algorithm that finds the "minimum length"/maximum coupling pathway between electron donors and acceptors in proteins J Am Chem Soc 114 4043 4046
    • (1992) J Am Chem Soc , vol.114 , pp. 4043-4046
    • Betts, J.N.1    Beratan, D.N.2    Onuchic, J.N.3
  • 21
    • 33748793395 scopus 로고    scopus 로고
    • The influence of the membrane potential on the protonation of bacteriorhodopsin: Insights from electrostatic calculations into the regulation of proton pumping
    • E Bombarda T Becker GM Ullmann 2006 The influence of the membrane potential on the protonation of bacteriorhodopsin: insights from electrostatic calculations into the regulation of proton pumping J Am Chem Soc 128 12129 12139
    • (2006) J Am Chem Soc , vol.128 , pp. 12129-12139
    • Bombarda, E.1    Becker, T.2    Ullmann, G.M.3
  • 22
    • 2342612092 scopus 로고    scopus 로고
    • Internal hydration of protein cavities: Studies on BPTI
    • A Borodich GM Ullmann 2004 Internal hydration of protein cavities: studies on BPTI PCCP 6 1906 1911
    • (2004) PCCP , vol.6 , pp. 1906-1911
    • Borodich, A.1    Ullmann, G.M.2
  • 24
    • 2442597248 scopus 로고    scopus 로고
    • The influence of a transmembrane pH gradient on protonation probabilities of bacteriorhodopsin: The structural basis of the back-pressure effect
    • N Calimet GM Ullmann 2004 The influence of a transmembrane pH gradient on protonation probabilities of bacteriorhodopsin: the structural basis of the back-pressure effect J Mol Biol 339 571 589
    • (2004) J Mol Biol , vol.339 , pp. 571-589
    • Calimet, N.1    Ullmann, G.M.2
  • 25
    • 33845698300 scopus 로고    scopus 로고
    • The architecture and function of the light-harvesting apparatus of purple bacteria: From single molecules to in vivo membranes
    • RJ Cogdell A Gall J Köhler 2006 The architecture and function of the light-harvesting apparatus of purple bacteria: from single molecules to in vivo membranes Q Rev Biophys 39 227 292
    • (2006) Q Rev Biophys , vol.39 , pp. 227-292
    • Cogdell, R.J.1    Gall, A.2    Köhler, J.3
  • 26
    • 0034480510 scopus 로고    scopus 로고
    • A cluster exposed: Structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins
    • CL Colbert MM-J Couture LD Eltis JT Bolin 2000 A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins Structure 8 1267 1278
    • (2000) Structure , vol.8 , pp. 1267-1278
    • Colbert, C.L.1    Mm-J, C.2    Eltis, L.D.3    Bolin, J.T.4
  • 27
    • 0035823820 scopus 로고    scopus 로고
    • Effects of pH on protein association. Modification of the proton linkage model and experimental verification of the modified model in the case of cytochrome c and plastocyanin
    • M Crnogorac GM Ullmann NM Kostić 2001 Effects of pH on protein association. Modification of the proton linkage model and experimental verification of the modified model in the case of cytochrome c and plastocyanin J Am Chem Soc 123 10789 10798
    • (2001) J Am Chem Soc , vol.123 , pp. 10789-10798
    • Crnogorac, M.1    Ullmann, G.M.2    Kostić, N.M.3
  • 29
    • 0035204346 scopus 로고    scopus 로고
    • Electrostatic analysis and Brownian dynamics simulation of the association of plastocyanin and cytochrome f.
    • F De Rienzo RRM Gabdoulline PGDB Cristina Menziani RC Wade 2001 Electrostatic analysis and Brownian dynamics simulation of the association of plastocyanin and cytochrome f. Biophys J 81 3090 3104
    • (2001) Biophys J , vol.81 , pp. 3090-3104
    • De Rienzo, F.1    Gabdoulline, R.R.M.2    Menziani Pgdb, C.3    Wade, R.C.4
  • 30
    • 0032502711 scopus 로고    scopus 로고
    • Alteration of the midpoint potential and catalytic activity of the Rieske iron-sulfur protein by changes of amino acids forming hydrogen bonds to the iron-sulfur cluster
    • 15
    • E Denke T Merbitz-Zahradnik OM Hatzfeld CH Snyder TA Link BL Trumpower 1998 Alteration of the midpoint potential and catalytic activity of the Rieske iron-sulfur protein by changes of amino acids forming hydrogen bonds to the iron-sulfur cluster J Biol Chem 273 15 9085 9093
    • (1998) J Biol Chem , vol.273 , pp. 9085-9093
    • Denke, E.1    Merbitz-Zahradnik, T.2    Hatzfeld, O.M.3    Snyder, C.H.4    Link, T.A.5    Trumpower, B.L.6
  • 31
    • 33846021303 scopus 로고    scopus 로고
    • Model for proton transport coupled to protein conformational change: Application to proton pumping in the bacteriorhodopsin photocycle
    • A Ferreira D Bashford 2006 Model for proton transport coupled to protein conformational change: application to proton pumping in the bacteriorhodopsin photocycle J Am Chem Soc 128 16778 16790
    • (2006) J Am Chem Soc , vol.128 , pp. 16778-16790
    • Ferreira, A.1    Bashford, D.2
  • 32
    • 0032054613 scopus 로고    scopus 로고
    • Quantum mechanical calculations on biological systems
    • RA Friesner MD Beachy 1998 Quantum mechanical calculations on biological systems Curr Opin Struct Biol 8 257 262
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 257-262
    • Friesner, R.A.1    Beachy, M.D.2
  • 34
    • 30744458117 scopus 로고    scopus 로고
    • Polarized FTIR spectroscopy in conjunction with in situ H/D exchange reveals the orientation of protein internal carboxylic acids
    • F Garczarek K Gerwert 2006 Polarized FTIR spectroscopy in conjunction with in situ H/D exchange reveals the orientation of protein internal carboxylic acids J Am Chem Soc 128 28 29
    • (2006) J Am Chem Soc , vol.128 , pp. 28-29
    • Garczarek, F.1    Gerwert, K.2
  • 36
    • 33646129211 scopus 로고    scopus 로고
    • A brownian dynamics study of the interaction of Phormidium cytochrome f with various cyanobacterial plastocyanins
    • EL Gross I Rosenberg 2006 A brownian dynamics study of the interaction of Phormidium cytochrome f with various cyanobacterial plastocyanins Biophys J 90 366 380
    • (2006) Biophys J , vol.90 , pp. 366-380
    • Gross, E.L.1    Rosenberg, I.2
  • 37
    • 0034640465 scopus 로고    scopus 로고
    • A pragmatic approach to structure based calculation of coupled proton and electron transfer in proteins
    • M Gunner 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.1    Alexov, E.2
  • 38
    • 33749189483 scopus 로고    scopus 로고
    • Factors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations
    • MR Gunner J Mao Y Song J Kim 2006 Factors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations Biochim Biophys Acta 1757 942 968
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 942-968
    • Gunner, M.R.1    Mao, J.2    Song, Y.3    Kim, J.4
  • 39
    • 21244491250 scopus 로고    scopus 로고
    • Brownian dynamics study of cytochrome f interactions with cytochrome c(6) and plastocyanin in Chlamydomonas reinhardtii plastocyanin, and cytochrome c(6) mutants
    • EJ Haddadian EL Gross 2005 Brownian dynamics study of cytochrome f interactions with cytochrome c(6) and plastocyanin in Chlamydomonas reinhardtii plastocyanin, and cytochrome c(6) mutants Biophys J 88 2323 2339
    • (2005) Biophys J , vol.88 , pp. 2323-2339
    • Haddadian, E.J.1    Gross, E.L.2
  • 40
    • 33646186478 scopus 로고    scopus 로고
    • 6 and plastocyanin in Chlamydomonas reinhardtii
    • 6 and plastocyanin in Chlamydomonas reinhardtii Biophys J 90 566 577
    • (2006) Biophys J , vol.90 , pp. 566-577
    • Haddadian, E.J.1    Gross, E.L.2
  • 42
    • 0032987196 scopus 로고    scopus 로고
    • Closing in on bacteriorhodopsin: Progress in understanding the molecule
    • U Haupts J Tittor D Oesterhelt 1999 Closing in on bacteriorhodopsin: progress in understanding the molecule Annu Rev Biophys Struct Biol 28 367 399
    • (1999) Annu Rev Biophys Struct Biol , vol.28 , pp. 367-399
    • Haupts, U.1    Tittor, J.2    Oesterhelt, D.3
  • 44
    • 0142151125 scopus 로고    scopus 로고
    • Electron transfer between membrane complexes and soluble proteins in photosynthesis
    • M Hervás JA Navarro MA DeLa Rosa 2003 Electron transfer between membrane complexes and soluble proteins in photosynthesis Acc Chem Res 36 798 805
    • (2003) Acc Chem Res , vol.36 , pp. 798-805
    • Hervás, M.1    Navarro, J.A.2    Dela Rosa, M.A.3
  • 47
    • 84987090159 scopus 로고
    • Molecular similarity based on electrostatic potential and electric field
    • E Hodgkin W Richards 1987 Molecular similarity based on electrostatic potential and electric field Int J Quant Chem Quant Biol Symp 14 105 110
    • (1987) Int J Quant Chem Quant Biol Symp , vol.14 , pp. 105-110
    • Hodgkin, E.1    Richards, W.2
  • 48
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • B Honig 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
  • 50
    • 0032096837 scopus 로고    scopus 로고
    • Continuum solvation model: Electrostatic forces from numerical solutions to the Poisson-Boltzmann equation
    • W Im D Beglov B Roux 1998 Continuum solvation model: electrostatic forces from numerical solutions to the Poisson-Boltzmann equation Comput Phys Commun 111 59 75
    • (1998) Comput Phys Commun , vol.111 , pp. 59-75
    • Im, W.1    Beglov, D.2    Roux, B.3
  • 51
    • 3042687860 scopus 로고    scopus 로고
    • B redox state in reaction centers from Rhodobacter sphaeroides
    • B redox state in reaction centers from Rhodobacter sphaeroides J Am Chem Soc 126 8059 8064
    • (2004) J Am Chem Soc , vol.126 , pp. 8059-8064
    • Ishikita, H.1    Knapp, E.-W.2
  • 52
    • 16844375171 scopus 로고    scopus 로고
    • Energetics of proton transfer pathways in reaction centers from Rhodobacter sphaeroides
    • H Ishiktia EW Knapp 2005 Energetics of proton transfer pathways in reaction centers from Rhodobacter sphaeroides J Biol Chem 280 12446 12450
    • (2005) J Biol Chem , vol.280 , pp. 12446-12450
    • Ishiktia, H.1    Knapp, E.W.2
  • 53
    • 0038258871 scopus 로고    scopus 로고
    • Effects of single and double mutations in plastocyanin on the rate constant and activation parameters of the gated electron-transfer reaction between the triplet state of zinc cytochrome c and cupriplastocyanin
    • MM Ivković-Jensen GM Ullmann S Young Ö Hansson M Crnogorac M Edjebäck NM Kostić 1998 Effects of single and double mutations in plastocyanin on the rate constant and activation parameters of the gated electron-transfer reaction between the triplet state of zinc cytochrome c and cupriplastocyanin Biochemistry 37 9557 9569
    • (1998) Biochemistry , vol.37 , pp. 9557-9569
    • Ivković-Jensen, M.M.1    Ullmann, G.M.2    Young, S.3    Hansson O.̈4    Crnogorac, M.5    Edjebäck, M.6    Kostić, N.M.7
  • 54
    • 0038573870 scopus 로고    scopus 로고
    • Comparing the rates and the activation parameters for the forward reaction between the triplet state of zinc cytochrome c and cupriplastocyanin and the back reaction between the zinc cytochrome c cation radical and cuproplastocyanin
    • MM Ivković-Jensen GM Ullmann MM Crnogorac M Ejdebäck S Young Ö Hansson NM Kostić 1999 Comparing the rates and the activation parameters for the forward reaction between the triplet state of zinc cytochrome c and cupriplastocyanin and the back reaction between the zinc cytochrome c cation radical and cuproplastocyanin Biochemistry 38 1589 1597
    • (1999) Biochemistry , vol.38 , pp. 1589-1597
    • Ivković-Jensen, M.M.1    Ullmann, G.M.2    Crnogorac, M.M.3    Ejdebäck, M.4    Young, S.5    Hansson O.̈6    Kostić, N.M.7
  • 56
    • 0035822679 scopus 로고    scopus 로고
    • Structural changes of Pharaonis phoborhodopsin upon photoisomerization of the retinal chromophore: Infrared spectral comparison with bacteriorhodopsin
    • H Kandori K Shimono Y Sudo M Iwamoto Y Shichida N Kamo 2001 Structural changes of Pharaonis phoborhodopsin upon photoisomerization of the retinal chromophore: infrared spectral comparison with bacteriorhodopsin Biochemistry 40 9238 9246
    • (2001) Biochemistry , vol.40 , pp. 9238-9246
    • Kandori, H.1    Shimono, K.2    Sudo, Y.3    Iwamoto, M.4    Shichida, Y.5    Kamo, N.6
  • 57
    • 4744343780 scopus 로고    scopus 로고
    • a values of Rieske iron-sulfur proteins
    • 39
    • a values of Rieske iron-sulfur proteins Biochemistry 43 39 12383 12389
    • (2004) Biochemistry , vol.43 , pp. 12383-12389
    • Klingen, A.R.1    Ullmann, G.M.2
  • 58
    • 33745099338 scopus 로고    scopus 로고
    • Theoretical investigation of the behavior of titratable groups in proteins
    • AR Klingen GM Ullmann 2006 Theoretical investigation of the behavior of titratable groups in proteins Photochem Photobiol Sci 5 588 596
    • (2006) Photochem Photobiol Sci , vol.5 , pp. 588-596
    • Klingen, A.R.1    Ullmann, G.M.2
  • 60
    • 28644443746 scopus 로고    scopus 로고
    • Electrostatic potential at the retinal of three archaeal rhodopsins: Implications for their different absorption spectra
    • E Kloppmann T Becker GM Ullmann 2005 Electrostatic potential at the retinal of three archaeal rhodopsins: implications for their different absorption spectra Proteins 61 953 965
    • (2005) Proteins , vol.61 , pp. 953-965
    • Kloppmann, E.1    Becker, T.2    Ullmann, G.M.3
  • 61
    • 34548580355 scopus 로고    scopus 로고
    • An extended dead-end elimination algorithm to determine gap-free lists of low energy states
    • E Kloppmann GM Ullmann T Becker 2007 An extended dead-end elimination algorithm to determine gap-free lists of low energy states J Comput Chem 28 2325 2335
    • (2007) J Comput Chem , vol.28 , pp. 2325-2335
    • Kloppmann, E.1    Ullmann, G.M.2    Becker, T.3
  • 62
    • 34447282051 scopus 로고    scopus 로고
    • PH modulates the quinone position in the photosynthetic reaction center from Rhodobacter sphaeroides in the neutral and charge separated states
    • J Koepke E-M Krammer AR Klingen P Sebban GM Ullmann G Fritzsch 2007 pH modulates the quinone position in the photosynthetic reaction center from Rhodobacter sphaeroides in the neutral and charge separated states J Mol Biol 371 396 409
    • (2007) J Mol Biol , vol.371 , pp. 396-409
    • Koepke, J.1    Krammer, E.-M.2    Klingen, A.R.3    Sebban, P.4    Ullmann, G.M.5    Fritzsch, G.6
  • 63
    • 0345017571 scopus 로고    scopus 로고
    • Dynamic aspects of electron-transfer reactions in metalloprotein complexes
    • Pittman CU (ed) Plenum Press, New York
    • Kostić NM (1996) Dynamic aspects of electron-transfer reactions in metalloprotein complexes. In: Pittman CU (ed) Metal-containing polymeric materials. Plenum Press, New York, pp 491-500
    • (1996) Metal-containing Polymeric Materials , pp. 491-500
    • Kostić, N.M.1
  • 64
    • 2342460436 scopus 로고    scopus 로고
    • Bacteriorhodopsin
    • JK Lanyi 2004 Bacteriorhodopsin Annu Rev Physiol 2004 665 688
    • (2004) Annu Rev Physiol , vol.2004 , pp. 665-688
    • Lanyi, J.K.1
  • 67
    • 0345453983 scopus 로고    scopus 로고
    • a values of hydrated transition metal cations by a combined density functional and continuum dielectric theory
    • a values of hydrated transition metal cations by a combined density functional and continuum dielectric theory J Phys Chem 96 2855 2866
    • (1996) J Phys Chem , vol.96 , pp. 2855-2866
    • Li, J.1    Fischer, C.L.2    Chen, J.L.3    Bashford, D.4    Noodleman, L.5
  • 68
    • 84962367570 scopus 로고    scopus 로고
    • Incorporating protein environments in density functional theory: A self-consistent reaction field calculation of redox potentials of [2Fe2S] clusters in ferredoxin and phthalate dioxygenase reductase
    • J Li MR Nelson CY Peng D Bashford L Noodleman 1998 Incorporating protein environments in density functional theory: a self-consistent reaction field calculation of redox potentials of [2Fe2S] clusters in ferredoxin and phthalate dioxygenase reductase J Phys Chem A 102 6311 6324
    • (1998) J Phys Chem a , vol.102 , pp. 6311-6324
    • Li, J.1    Nelson, M.R.2    Peng, C.Y.3    Bashford, D.4    Noodleman, L.5
  • 69
    • 33747797654 scopus 로고    scopus 로고
    • Rieske protein from Thermus thermophilus: (15)N NMR titration study demonstrates the role of iron-ligated histidines in the pH dependence of the reduction potential
    • IJ Lin Y Chen JA Fee J Song WM Westler JL Markley 2006 Rieske protein from Thermus thermophilus: (15)N NMR titration study demonstrates the role of iron-ligated histidines in the pH dependence of the reduction potential J Am Chem Soc 128 10672 10673
    • (2006) J Am Chem Soc , vol.128 , pp. 10672-10673
    • Lin, I.J.1    Chen, Y.2    Fee, J.A.3    Song, J.4    Westler, W.M.5    Markley, J.L.6
  • 70
    • 0028220770 scopus 로고
    • Two pK values of the oxidized Rieske [2Fe-2S] cluster observed by CD spectroscopy
    • TA Link 1994 Two pK values of the oxidized Rieske [2Fe-2S] cluster observed by CD spectroscopy Biochim Biophys Acta 1185 81 84
    • (1994) Biochim Biophys Acta , vol.1185 , pp. 81-84
    • Link, T.A.1
  • 71
    • 2342637738 scopus 로고    scopus 로고
    • Density functional vertical self-consistent reaction field theory for solvatochromism studies of solvent-sensitive dyes
    • T Liu W-G Han F Himo GM Ullmann D Bashford A Toutchkine KM Hahn L Noodleman 2004 Density functional vertical self-consistent reaction field theory for solvatochromism studies of solvent-sensitive dyes J Phys Chem B 108 11157 11169
    • (2004) J Phys Chem B , vol.108 , pp. 11157-11169
    • Liu, T.1    Han, W.-G.2    Himo, F.3    Ullmann, G.M.4    Bashford, D.5    Toutchkine, A.6    Hahn, K.M.7    Noodleman, L.8
  • 73
    • 0035943457 scopus 로고    scopus 로고
    • Crystal structure of sensory rhodopsin II at 2.4 angstroms: Insights into color tuning and transducer interaction
    • H Luecke B Schobert JK Lanyi EN Spudich JL Spudich 2001 Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction Science 293 1499 1502
    • (2001) Science , vol.293 , pp. 1499-1502
    • Luecke, H.1    Schobert, B.2    Lanyi, J.K.3    Spudich, E.N.4    Spudich, J.L.5
  • 74
    • 0036771626 scopus 로고    scopus 로고
    • Accelerated Poisson-Boltzmann calculations for static and dynamic systems
    • R Luo L David MK Gilson 2002 Accelerated Poisson-Boltzmann calculations for static and dynamic systems J Comput Chem 23 1244 1253
    • (2002) J Comput Chem , vol.23 , pp. 1244-1253
    • Luo, R.1    David, L.2    Gilson, M.K.3
  • 75
    • 33748768973 scopus 로고    scopus 로고
    • Interpigment Coulomb couplings from ab-initio transition charges: Application to strongly coupled pigments in photosynthetic antennae and reaction centers
    • ME Madjet A Abdurahman T Renger 2006 Interpigment Coulomb couplings from ab-initio transition charges: application to strongly coupled pigments in photosynthetic antennae and reaction centers J Phys Chem B 110 17268
    • (2006) J Phys Chem B , vol.110 , pp. 17268
    • Madjet, M.E.1    Abdurahman, A.2    Renger, T.3
  • 77
    • 0000378873 scopus 로고
    • Free energy of nonequilibrium polarization systems. II. Homogeneous and electrode systems
    • RA Marcus 1963 Free energy of nonequilibrium polarization systems. II. Homogeneous and electrode systems J Chem Phys 38 1858 1862
    • (1963) J Chem Phys , vol.38 , pp. 1858-1862
    • Marcus, R.A.1
  • 78
    • 0022004980 scopus 로고
    • Electron transfer in chemistry and biology
    • RA Marcus N Sutin 1985 Electron transfer in chemistry and biology Biochim Biophys Acta 811 265 322
    • (1985) Biochim Biophys Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 82
    • 0042011188 scopus 로고    scopus 로고
    • Calculating pKa values in enzyme active sites
    • JE Nielsen JA McCammon 2003 Calculating pKa values in enzyme active sites Protein Sci 12 1894 1901
    • (2003) Protein Sci , vol.12 , pp. 1894-1901
    • Nielsen, J.E.1    McCammon, J.A.2
  • 83
    • 0028266377 scopus 로고
    • Hydrodynamic motions of large molecules
    • SH Northrup 1994 Hydrodynamic motions of large molecules Curr Opin Struct Biol 4 269 274
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 269-274
    • Northrup, S.H.1
  • 84
    • 36549102274 scopus 로고
    • Brownian dynamics simulation of diffusion-influenced bimolecular reactions
    • SH Northrup SA Allison JA McCammon 1984 Brownian dynamics simulation of diffusion-influenced bimolecular reactions J Chem Phys 80 1517 1524
    • (1984) J Chem Phys , vol.80 , pp. 1517-1524
    • Northrup, S.H.1    Allison, S.A.2    McCammon, J.A.3
  • 86
    • 34047206090 scopus 로고    scopus 로고
    • Quantum chemical calculation of the reorganization energy of blue copper proteins
    • MHM Olsson U Ryde BO Roos 1998 Quantum chemical calculation of the reorganization energy of blue copper proteins Protein Sci 81 6554 6558
    • (1998) Protein Sci , vol.81 , pp. 6554-6558
    • Olsson, M.H.M.1    Ryde, U.2    Roos, B.O.3
  • 87
    • 4043068022 scopus 로고    scopus 로고
    • Decomposing complex ligand binding into simple components: Connections between microscopic and macroscopic models
    • A Onufriev GM Ullmann 2004 Decomposing complex ligand binding into simple components: connections between microscopic and macroscopic models J Phys Chem B 108 11157 11169
    • (2004) J Phys Chem B , vol.108 , pp. 11157-11169
    • Onufriev, A.1    Ullmann, G.M.2
  • 88
    • 0035957234 scopus 로고    scopus 로고
    • A novel view on the pH titration of biomolecules
    • A Onufriev DA Case GM Ullmann 2001 A novel view on the pH titration of biomolecules Biochemistry 40 3413 3419
    • (2001) Biochemistry , vol.40 , pp. 3413-3419
    • Onufriev, A.1    Case, D.A.2    Ullmann, G.M.3
  • 89
    • 0042386423 scopus 로고    scopus 로고
    • Proton affinity changes driving unidirectional proton transport in the bacteriorhodopsin photocycle
    • A Onufriev A Smondyrev D Bashford 2003 Proton affinity changes driving unidirectional proton transport in the bacteriorhodopsin photocycle J Mol Biol 332 1183 1193
    • (2003) J Mol Biol , vol.332 , pp. 1183-1193
    • Onufriev, A.1    Smondyrev, A.2    Bashford, D.3
  • 90
    • 0027535989 scopus 로고
    • Electron transfer from the tetraheme cytochrome to the special pair in isolated reaction centers of Rhodopseudomonas viridis
    • JM Ortega P Mathis 1993 Electron transfer from the tetraheme cytochrome to the special pair in isolated reaction centers of Rhodopseudomonas viridis Biochemistry 32 1141 1151
    • (1993) Biochemistry , vol.32 , pp. 1141-1151
    • Ortega, J.M.1    Mathis, P.2
  • 92
    • 0024726467 scopus 로고
    • Pathway of proton transfer in bacterial reaction centers: Replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover
    • ML Paddock SH Rongley G Feher MY Okamura 1989 Pathway of proton transfer in bacterial reaction centers: replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover Proc Natl Acad Sci USA 86 6602 6606
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6602-6606
    • Paddock, M.L.1    Rongley, S.H.2    Feher, G.3    Okamura, M.Y.4
  • 93
    • 0025134851 scopus 로고
    • 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
    • ML Paddock PH McPherson G Feher MY Okamura 1990 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 Proc Natl Acad Sci USA 87 6803 6807
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6803-6807
    • Paddock, M.L.1    McPherson, P.H.2    Feher, G.3    Okamura, M.Y.4
  • 94
    • 0028009920 scopus 로고
    • Pathway of proton transfer in bacterial reaction centers: Role of Aspartate-L213 in proton transfers associated with reduction of quinone to dihydroquinone
    • ML Paddock SH Rongey PH McPherson A Juth G Feher M Yokamura 1994 Pathway of proton transfer in bacterial reaction centers: role of Aspartate-L213 in proton transfers associated with reduction of quinone to dihydroquinone Biochemistry 33 734 745
    • (1994) Biochemistry , vol.33 , pp. 734-745
    • Paddock, M.L.1    Rongey, S.H.2    McPherson, P.H.3    Juth, A.4    Feher, G.5    Yokamura, M.6
  • 98
    • 0242657390 scopus 로고    scopus 로고
    • Proton transfer pathways and mechanism in bacterial reaction centers
    • ML Paddock G Feher MY Okamura 2003 Proton transfer pathways and mechanism in bacterial reaction centers FEBS Lett 555 45 50
    • (2003) FEBS Lett , vol.555 , pp. 45-50
    • Paddock, M.L.1    Feher, G.2    Okamura, M.Y.3
  • 99
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunneling in biological oxidation-reduction
    • CC Page CC Moser X Chen PL Dutton 1999 Natural engineering principles of electron tunneling in biological oxidation-reduction Nature 402 47 52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 100
    • 0344573439 scopus 로고
    • The docking of cytochrome f with plastocyanin: Three possible complexes
    • Mathis P (ed) Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Pearson DC, Gross EL (1995) The docking of cytochrome f with plastocyanin: three possible complexes. In: Mathis P (ed) Photosynthesis: from light to biosphere, vol II. Kluwer Academic Publishers, Dordrecht, The Netherlands, pp 729-732
    • (1995) Photosynthesis: From Light to Biosphere , vol.2 , pp. 729-732
    • Pearson, D.C.1    Gross, E.L.2
  • 101
    • 8944236999 scopus 로고    scopus 로고
    • Electrostatic properties of cytochrome f: Implications for docking with plastocyanin
    • DC Pearson EL Gross E David 1996 Electrostatic properties of cytochrome f: implications for docking with plastocyanin Biophys J 71 64 76
    • (1996) Biophys J , vol.71 , pp. 64-76
    • Pearson, D.C.1    Gross, E.L.2    David, E.3
  • 102
    • 9244259076 scopus 로고    scopus 로고
    • Implementation and testing of stable, fast implicit solvation in molecular dynamics using the smooth-permittivity finite difference Poisson-Boltzmann method
    • NV Prabhu P Zhu KA Sharp 2004 Implementation and testing of stable, fast implicit solvation in molecular dynamics using the smooth-permittivity finite difference Poisson-Boltzmann method J Comput Chem 25 2049 2064
    • (2004) J Comput Chem , vol.25 , pp. 2049-2064
    • Prabhu, N.V.1    Zhu, P.2    Sharp, K.A.3
  • 103
    • 0027263613 scopus 로고
    • Importance of protein rearrangement in the electron-transfer reaction between the physiological partners cytochrome f and plastocyanin
    • L Qin NM Kostić 1993 Importance of protein rearrangement in the electron-transfer reaction between the physiological partners cytochrome f and plastocyanin Biochemistry 32 6073 6080
    • (1993) Biochemistry , vol.32 , pp. 6073-6080
    • Qin, L.1    Kostić, N.M.2
  • 104
    • 0031719963 scopus 로고    scopus 로고
    • Calculation of protonation patterns in proteins with structural relaxation and molecular ensembles-application to the photosynthetic reaction center
    • B Rabenstein GM Ullmann 1998 Calculation of protonation patterns in proteins with structural relaxation and molecular ensembles-application to the photosynthetic reaction center Eur Biophys J 27 626 637
    • (1998) Eur Biophys J , vol.27 , pp. 626-637
    • Rabenstein, B.1    Ullmann, G.M.2
  • 105
    • 0032562210 scopus 로고    scopus 로고
    • Energetics of electron-transfer and protonation reactions of the quinones in the photosynthetic reaction center of Rhodopseudomonas viridis
    • B Rabenstein GM Ullmann EW 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
  • 106
    • 0034730115 scopus 로고    scopus 로고
    • Electron transfer between the quinones in the photosynthetic reaction center and its coupling to conformational changes
    • B Rabenstein GM Ullmann EW Knapp 2000 Electron transfer between the quinones in the photosynthetic reaction center and its coupling to conformational changes Biochemistry 39 10496 10587
    • (2000) Biochemistry , vol.39 , pp. 10496-10587
    • Rabenstein, B.1    Ullmann, G.M.2    Knapp, E.W.3
  • 107
    • 3643084753 scopus 로고
    • The absolute potential of the standard hydrogen electrode: A new estimate
    • H Reiss A Heller 1985 The absolute potential of the standard hydrogen electrode: a new estimate J Phys Chem 89 4207 4213
    • (1985) J Phys Chem , vol.89 , pp. 4207-4213
    • Reiss, H.1    Heller, A.2
  • 109
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • FM Richards 1977 Areas, volumes, packing and protein structure Annu Rev Biophys Bioeng 6 151 176
    • (1977) Annu Rev Biophys Bioeng , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 111
    • 0025861597 scopus 로고
    • Electrostatic orientation of the electron-transfer complex between plastocyanin and cytochrome c
    • VA Roberts HC Freeman AJ Olson JA Tainer ED Getzoff 1991 Electrostatic orientation of the electron-transfer complex between plastocyanin and cytochrome c J Biol Chem 266 13431 13441
    • (1991) J Biol Chem , vol.266 , pp. 13431-13441
    • Roberts, V.A.1    Freeman, H.C.2    Olson, A.J.3    Tainer, J.A.4    Getzoff, E.D.5
  • 112
    • 0030735981 scopus 로고    scopus 로고
    • The influence of the membrane potential on the free energy of an intrinsic protein
    • B Roux 1997 The influence of the membrane potential on the free energy of an intrinsic protein Biophys J 73 2981 2989
    • (1997) Biophys J , vol.73 , pp. 2981-2989
    • Roux, B.1
  • 114
    • 0035252132 scopus 로고    scopus 로고
    • Structure, strain and reorganization energy of blue copper models in the protein.
    • U Ryde MHM Olsson 2001 Structure, strain and reorganization energy of blue copper models in the protein. Int J Quant Chem 81 335 347
    • (2001) Int J Quant Chem , vol.81 , pp. 335-347
    • Ryde, U.1    Olsson, M.H.M.2
  • 115
    • 0032406917 scopus 로고    scopus 로고
    • Evidence for the archaebacterial-type conformation about the bond between the small β-ionone ring and the polyene chain of the chromophore retinal in chlamyrhodopsin
    • M Sakamoto A Wada A Akai M Ito T Goshima T Takahashi 1998 Evidence for the archaebacterial-type conformation about the bond between the small β-ionone ring and the polyene chain of the chromophore retinal in chlamyrhodopsin FEBS Lett 434 335 338
    • (1998) FEBS Lett , vol.434 , pp. 335-338
    • Sakamoto, M.1    Wada, A.2    Akai, A.3    Ito, M.4    Goshima, T.5    Takahashi, T.6
  • 116
    • 0028218956 scopus 로고
    • Environmental effects on the protonation states of active site residues in bacteriorhodopsin
    • RV Sampogna B Honig 1994 Environmental effects on the protonation states of active site residues in bacteriorhodopsin Biophys J 66 1341 1352
    • (1994) Biophys J , vol.66 , pp. 1341-1352
    • Sampogna, R.V.1    Honig, B.2
  • 117
    • 0029781697 scopus 로고    scopus 로고
    • Electrostatic coupling between retinal isomerization and the ionization state of Glu-204: A general mechanism for proton release in bacteriorhodopsin
    • RV Sampogna B Honig 1996 Electrostatic coupling between retinal isomerization and the ionization state of Glu-204: a general mechanism for proton release in bacteriorhodopsin Biophys J 71 1165 1171
    • (1996) Biophys J , vol.71 , pp. 1165-1171
    • Sampogna, R.V.1    Honig, B.2
  • 118
    • 84987064337 scopus 로고
    • Proton release pathway in bacteriorhodopsin: Molecular dynamics and electrostatic calculations
    • C Scharnagl J Hettenkofer SF Fischer 1994 Proton release pathway in bacteriorhodopsin: molecular dynamics and electrostatic calculations Int J Quant Chem 52 33 56
    • (1994) Int J Quant Chem , vol.52 , pp. 33-56
    • Scharnagl, C.1    Hettenkofer, J.2    Fischer, S.F.3
  • 119
    • 0028787627 scopus 로고
    • Electron and proton transfer to the quinones in bacterial photosynthetic reaction centers: Insight from combined approaches of molecular genetics and biophysics
    • P Sebban P Maróti DK Hanson 1995 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
    • (1995) Biochimie , vol.77 , pp. 677-694
    • Sebban, P.1    Maróti, P.2    Hanson, D.K.3
  • 124
    • 0344418714 scopus 로고    scopus 로고
    • Simulating proton translocations in proteins: Probing proton transfer pathways in the Rhodobacter sphaeroides reaction center
    • YY Sham I Muegge A Warshel 1999 Simulating proton translocations in proteins: probing proton transfer pathways in the Rhodobacter sphaeroides reaction center Proteins 36 484 500
    • (1999) Proteins , vol.36 , pp. 484-500
    • Sham, Y.Y.1    Muegge, I.2    Warshel, A.3
  • 125
    • 0031886681 scopus 로고    scopus 로고
    • Calculation of electron transfer reorganization energies using the Finite Difference Poisson-Boltzmann model
    • KE Sharp 1998 Calculation of electron transfer reorganization energies using the Finite Difference Poisson-Boltzmann model Biophys J 73 1241 1250
    • (1998) Biophys J , vol.73 , pp. 1241-1250
    • Sharp, K.E.1
  • 126
    • 0032956179 scopus 로고    scopus 로고
    • Electrostatic effects on the kinetics of photoinduced electron-transfer reactions of the triplet state of zinc cytochrome c with wild-type and mutant forms of Pseudomonas aeruginosa azurin
    • EV Sokerina GM Ullmann G van Pouderoyen GW Canters NM Kostić 1999 Electrostatic effects on the kinetics of photoinduced electron-transfer reactions of the triplet state of zinc cytochrome c with wild-type and mutant forms of Pseudomonas aeruginosa azurin J Biol Inorg Chem 4 111 121
    • (1999) J Biol Inorg Chem , vol.4 , pp. 111-121
    • Sokerina, E.V.1    Ullmann, G.M.2    Van Pouderoyen, G.3    Canters, G.W.4    Kostić, N.M.5
  • 127
    • 0041471589 scopus 로고    scopus 로고
    • Calculation of proton transfers in bacteriorhodopsin bR and M intermediates
    • Y Song J Mao MR Gunner 2003 Calculation of proton transfers in bacteriorhodopsin bR and M intermediates Biochemistry 42 9875 9888
    • (2003) Biochemistry , vol.42 , pp. 9875-9888
    • Song, Y.1    Mao, J.2    Gunner, M.R.3
  • 128
    • 0035823064 scopus 로고    scopus 로고
    • a calculations suggest storage of an excess proton in a hydrogen-bonded water network in bacteriorhodopsin
    • a calculations suggest storage of an excess proton in a hydrogen-bonded water network in bacteriorhodopsin J Mol Biol 312 203 219
    • (2001) J Mol Biol , vol.312 , pp. 203-219
    • Spassov, V.Z.1    Luecke, H.2    Gerwert, K.3    Bashford, D.4
  • 129
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron-proton transfer
    • MHV Stowell TM McPhillips DC Rees SM Soltis E Abresch 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.V.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 132
    • 4043055221 scopus 로고    scopus 로고
    • Complexes of photosynthetic redox proteins studied by NMR
    • M Ubbink 2004 Complexes of photosynthetic redox proteins studied by NMR Photosyn Res 81 277 287
    • (2004) Photosyn Res , vol.81 , pp. 277-287
    • Ubbink, M.1
  • 133
    • 0032520957 scopus 로고    scopus 로고
    • The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid body molecular dynamics
    • M Ubbink M Ejdebäck BG Karlson DS Bendall 1998 The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid body molecular dynamics Structure 6 323 335
    • (1998) Structure , vol.6 , pp. 323-335
    • Ubbink, M.1    Ejdebäck, M.2    Karlson, B.G.3    Bendall, D.S.4
  • 135
    • 0037421933 scopus 로고    scopus 로고
    • Relations between protonation constants and titration curves in polyprotic acids: A critical view
    • GM Ullmann 2003 Relations between protonation constants and titration curves in polyprotic acids: a critical view J Phys Chem B 107 6293 6301
    • (2003) J Phys Chem B , vol.107 , pp. 6293-6301
    • Ullmann, G.M.1
  • 136
    • 0001337688 scopus 로고
    • Electron-tunneling paths in various electrostatic complexes between cytochrome c and plastocyanin. Anisotropy of the copper-ligand interactions and dependence of the iron-copper electronic coupling on the metalloprotein orientation
    • GM Ullmann NM Kostić 1995 Electron-tunneling paths in various electrostatic complexes between cytochrome c and plastocyanin. Anisotropy of the copper-ligand interactions and dependence of the iron-copper electronic coupling on the metalloprotein orientation J Am Chem Soc 117 4766 4774
    • (1995) J Am Chem Soc , vol.117 , pp. 4766-4774
    • Ullmann, G.M.1    Kostić, N.M.2
  • 137
    • 0000000699 scopus 로고    scopus 로고
    • Electrostatic Computations of protonation and redox equilibria in proteins
    • GM Ullmann EW Knapp 1999 Electrostatic Computations of 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
  • 139
    • 0031041540 scopus 로고    scopus 로고
    • Computational simulation and analysis of the dynamic association between plastocyanin and cytochrome f. Consequences for the electron-transfer reaction
    • GM Ullmann EW Knapp NM Kostić 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    Kostić, N.M.3
  • 140
    • 0034651549 scopus 로고    scopus 로고
    • Superposition of ferredoxin and flavodoxin using their electrostatic potentials. Implications for their interactions with photosystem I and ferredoxin:NADP reductase
    • GM Ullmann M Hauswald A Jensen EW Knapp 2000 Superposition of ferredoxin and flavodoxin using their electrostatic potentials. Implications for their interactions with photosystem I and ferredoxin:NADP reductase Proteins 38 301 309
    • (2000) Proteins , vol.38 , pp. 301-309
    • Ullmann, G.M.1    Hauswald, M.2    Jensen, A.3    Knapp, E.W.4
  • 141
  • 143
    • 0000825914 scopus 로고    scopus 로고
    • Electron transfer and proton coupling in proteins
    • RJP Williams 1999 Electron transfer and proton coupling in proteins J Solid State Chem 145 488 495
    • (1999) J Solid State Chem , vol.145 , pp. 488-495
    • Williams, R.J.P.1
  • 144
    • 0000253530 scopus 로고
    • Gating of the photoinduced electron transfer from zinc cytochrome c and tin cytochrome c to plastocyanin. Effects of the solution viscosity on the rearrangement of the metalloproteins
    • JS Zhou NM Kostić 1993 Gating of the photoinduced electron transfer from zinc cytochrome c and tin cytochrome c to plastocyanin. Effects of the solution viscosity on the rearrangement of the metalloproteins J Am Chem Soc 115 10796 10804
    • (1993) J Am Chem Soc , vol.115 , pp. 10796-10804
    • Zhou, J.S.1    Kostić, N.M.2
  • 145
    • 0035840956 scopus 로고    scopus 로고
    • Complete thermodynamic characterization of reduction and protonation of the bc1-type Rieske [2Fe-2S] center of Thermus thermophilus
    • Y Zu JA Fee J Hirst 2001 Complete thermodynamic characterization of reduction and protonation of the bc1-type Rieske [2Fe-2S] center of Thermus thermophilus J Biol Chem 276 9906 9907
    • (2001) J Biol Chem , vol.276 , pp. 9906-9907
    • Zu, Y.1    Fee, J.A.2    Hirst, J.3


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