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Volumn 1827, Issue 3, 2013, Pages 328-339

Effects of dehydration on light-induced conformational changes in bacterial photosynthetic reaction centers probed by optical and differential FTIR spectroscopy

Author keywords

Bacterial reaction center; Charge recombination; Conformational dynamics; Dielectric relaxation; Difference FTIR spectroscopy; Protein hydration

Indexed keywords

WATER;

EID: 84871945799     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2012.10.009     Document Type: Article
Times cited : (28)

References (65)
  • 1
    • 0000058886 scopus 로고
    • Structure and function of bacterial photosynthetic reaction centres
    • G. Feher, J.P. Allen, M.Y. Okamura, and D.C. Rees Structure and function of bacterial photosynthetic reaction centres Nature 33 1989 111 116
    • (1989) Nature , vol.33 , pp. 111-116
    • Feher, G.1    Allen, J.P.2    Okamura, M.Y.3    Rees, D.C.4
  • 2
    • 1242347393 scopus 로고    scopus 로고
    • Proton and electron transfer in the acceptor quinone complex of photosynthetic reaction centers from Rhodobacter sphaeroides
    • C.A. Wraight Proton and electron transfer in the acceptor quinone complex of photosynthetic reaction centers from Rhodobacter sphaeroides Front. Biosci. 9 2004 309 337
    • (2004) Front. Biosci. , vol.9 , pp. 309-337
    • Wraight, C.A.1
  • 3
    • 0019878636 scopus 로고
    • Enthalpy and volume changes accompanying electron transfer from P-870 to quinones in Rhodopseudomonas sphaeroides reaction centers
    • H. Arata, and W.W. Parson Enthalpy and volume changes accompanying electron transfer from P-870 to quinones in Rhodopseudomonas sphaeroides reaction centers Biochim. Biophys. Acta 636 1981 70 81
    • (1981) Biochim. Biophys. Acta , vol.636 , pp. 70-81
    • Arata, H.1    Parson, W.W.2
  • 4
    • 0021674417 scopus 로고
    • Electron transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: Evidence for light-induced structural changes
    • D. Kleinfeld, M.Y. Okamura, and G. Feher Electron transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: evidence for light-induced structural changes Biochemistry 23 1984 5780 5786
    • (1984) Biochemistry , vol.23 , pp. 5780-5786
    • Kleinfeld, D.1    Okamura, M.Y.2    Feher, G.3
  • 5
    • 0025292657 scopus 로고
    • A protein conformational change associated with the photoreduction of the primary and secondary quinones in the bacterial reaction center
    • E. Nabedryk, K.A. Bagley, D.L. Thibodeau, M. Bauscher, W. Mäntele, and J. Breton A protein conformational change associated with the photoreduction of the primary and secondary quinones in the bacterial reaction center FEBS Lett. 266 1990 59 62
    • (1990) FEBS Lett. , vol.266 , pp. 59-62
    • Nabedryk, E.1    Bagley, K.A.2    Thibodeau, D.L.3    Bauscher, M.4    Mäntele, W.5    Breton, J.6
  • 6
    • 0029016874 scopus 로고
    • Trypsin treatment of reaction centers from Rhodobacter sphaeroides in the dark and under illumination: Protein structural changes follow charge separation
    • P. Brzezinski, and L.E. Andréasson Trypsin treatment of reaction centers from Rhodobacter sphaeroides in the dark and under illumination: protein structural changes follow charge separation Biochemistry 34 1995 7498 7506
    • (1995) Biochemistry , vol.34 , pp. 7498-7506
    • Brzezinski, P.1    Andréasson, L.E.2
  • 7
    • 0344193626 scopus 로고    scopus 로고
    • Electron transfer and protein dynamics in the photosynthetic reaction center
    • B.H. McMahon, J.D. Müller, C.A. Wraight, and G.U. Nienhaus Electron transfer and protein dynamics in the photosynthetic reaction center Biophys. J. 74 1998 2567 2587
    • (1998) Biophys. J. , vol.74 , pp. 2567-2587
    • McMahon, B.H.1    Müller, J.D.2    Wraight, C.A.3    Nienhaus, G.U.4
  • 8
    • 17144438827 scopus 로고    scopus 로고
    • Characterization of a semi-stable, charge-separated state in reaction centers from Rhodobacter sphaeroides
    • U. Andréasson, and L.-E. Andréasson Characterization of a semi-stable, charge-separated state in reaction centers from Rhodobacter sphaeroides Photosynth. Res. 75 2003 223 233
    • (2003) Photosynth. Res. , vol.75 , pp. 223-233
    • Andréasson, U.1    Andréasson, L.-E.2
  • 11
    • 79959938255 scopus 로고    scopus 로고
    • Charge recombination time distributions in photosynthetic reaction centers exposed to alternating intervals of photoexcitation and dark relaxation
    • A.J. Manzo, A.O. Goushcha, N.M. Berezetska, V.N. Kharkyanen, and G.W. Scott Charge recombination time distributions in photosynthetic reaction centers exposed to alternating intervals of photoexcitation and dark relaxation J. Phys. Chem. B 115 2011 8534 8544
    • (2011) J. Phys. Chem. B , vol.115 , pp. 8534-8544
    • Manzo, A.J.1    Goushcha, A.O.2    Berezetska, N.M.3    Kharkyanen, V.N.4    Scott, G.W.5
  • 12
    • 78751536387 scopus 로고    scopus 로고
    • Light-induced conformational changes in photosynthetic reaction centers: Dielectric relaxation in the vicinity of the dimer
    • S.S. Deshmukh, J.C. Williams, J.P. Allen, and L. Kálmán Light-induced conformational changes in photosynthetic reaction centers: dielectric relaxation in the vicinity of the dimer Biochemistry 50 2011 340 348
    • (2011) Biochemistry , vol.50 , pp. 340-348
    • Deshmukh, S.S.1    Williams, J.C.2    Allen, J.P.3    Kálmán, L.4
  • 13
    • 79955094713 scopus 로고    scopus 로고
    • Light-induced conformational changes in photosynthetic reaction centers: Redox-regulated proton pathway near the dimer
    • S.S. Deshmukh, J.C. Williams, J.P. Allen, and L. Kálmán Light-induced conformational changes in photosynthetic reaction centers: redox-regulated proton pathway near the dimer Biochemistry 50 2011 3321 3331
    • (2011) Biochemistry , vol.50 , pp. 3321-3331
    • Deshmukh, S.S.1    Williams, J.C.2    Allen, J.P.3    Kálmán, L.4
  • 14
    • 0038479088 scopus 로고    scopus 로고
    • Conformation-activated protonation in reaction centers of the photosynthetic bacterium Rhodobacter sphaeroides
    • L. Kálmán, and P. Maróti Conformation-activated protonation in reaction centers of the photosynthetic bacterium Rhodobacter sphaeroides Biochemistry 36 1997 15269 15276
    • (1997) Biochemistry , vol.36 , pp. 15269-15276
    • Kálmán, L.1    Maróti, P.2
  • 15
    • 0035795148 scopus 로고    scopus 로고
    • Long-lived charge-separated states in bacterial reaction centers isolated from Rhodobacter sphaeroides
    • F. Van Mourik, M. Reus, and A.R. Holzwarth Long-lived charge-separated states in bacterial reaction centers isolated from Rhodobacter sphaeroides Biochim. Biophys. Acta 1504 2001 311 318
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 311-318
    • Van Mourik, F.1    Reus, M.2    Holzwarth, A.R.3
  • 18
    • 0041622652 scopus 로고    scopus 로고
    • Coupling of light-induced electron transfer to proton uptake in photosynthesis
    • A. Remy, and K. Gerwert Coupling of light-induced electron transfer to proton uptake in photosynthesis Nat. Struct. Biol. 10 2003 637 644
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 637-644
    • Remy, A.1    Gerwert, K.2
  • 19
    • 64349113842 scopus 로고    scopus 로고
    • Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from Rhodobacter sphaeroides
    • T. Iwata, M.L. Paddock, M.Y. Okamura, and H. Kandori Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from Rhodobacter sphaeroides Biochemistry 48 2009 1220 1229
    • (2009) Biochemistry , vol.48 , pp. 1220-1229
    • Iwata, T.1    Paddock, M.L.2    Okamura, M.Y.3    Kandori, H.4
  • 20
    • 83455195600 scopus 로고    scopus 로고
    • Coupling between electron transfer and protein solvent dynamics: FTIR and laser-flash spectroscopy studies in photosynthetic reaction center films at different hydration levels
    • M. Malferrari, F. Francia, and G. Venturoli Coupling between electron transfer and protein solvent dynamics: FTIR and laser-flash spectroscopy studies in photosynthetic reaction center films at different hydration levels J. Phys. Chem. B 115 2011 14732 14750
    • (2011) J. Phys. Chem. B , vol.115 , pp. 14732-14750
    • Malferrari, M.1    Francia, F.2    Venturoli, G.3
  • 21
    • 0036156512 scopus 로고    scopus 로고
    • Electron transfer kinetics in photosynthetic reaction centers embedded in trehalose glasses: Trapping of conformational substates at room temperature
    • G. Palazzo, A. Mallardi, A. Hochkoeppler, L. Cordone, and G. Venturoli Electron transfer kinetics in photosynthetic reaction centers embedded in trehalose glasses: trapping of conformational substates at room temperature Biophys. J. 82 2002 558 568
    • (2002) Biophys. J. , vol.82 , pp. 558-568
    • Palazzo, G.1    Mallardi, A.2    Hochkoeppler, A.3    Cordone, L.4    Venturoli, G.5
  • 22
    • 3543046791 scopus 로고    scopus 로고
    • Probing light-induced conformational transitions in bacterial photosynthetic reaction centers embedded in trehalose-water amorphous matrices
    • F. Francia, G. Palazzo, A. Mallardi, L. Cordone, and G. Venturoli Probing light-induced conformational transitions in bacterial photosynthetic reaction centers embedded in trehalose-water amorphous matrices Biochim. Biophys. Acta 1658 2004 50 57
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 50-57
    • Francia, F.1    Palazzo, G.2    Mallardi, A.3    Cordone, L.4    Venturoli, G.5
  • 23
    • 48749094210 scopus 로고    scopus 로고
    • Protein-matrix coupling/uncoupling in "dry" systems of photosynthetic reaction center embedded in trehalose/sucrose: The origin of trehalose peculiarity
    • F. Francia, M. Dezi, A. Mallardi, G. Palazzo, L. Cordone, and G. Venturoli Protein-matrix coupling/uncoupling in "dry" systems of photosynthetic reaction center embedded in trehalose/sucrose: the origin of trehalose peculiarity J. Am. Chem. Soc. 130 2008 10240 10246
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 10240-10246
    • Francia, F.1    Dezi, M.2    Mallardi, A.3    Palazzo, G.4    Cordone, L.5    Venturoli, G.6
  • 24
    • 67651207530 scopus 로고    scopus 로고
    • Charge recombination kinetics and protein dynamics in wild type and carotenoid-less bacterial reaction centers: Studies in trehalose glasses
    • F. Francia, M. Malferrari, S. Sacquin-Mora, and G. Venturoli Charge recombination kinetics and protein dynamics in wild type and carotenoid-less bacterial reaction centers: studies in trehalose glasses J. Phys. Chem. B 113 2009 10389 10398
    • (2009) J. Phys. Chem. B , vol.113 , pp. 10389-10398
    • Francia, F.1    Malferrari, M.2    Sacquin-Mora, S.3    Venturoli, G.4
  • 25
    • 77957303680 scopus 로고    scopus 로고
    • Bacterial photosynthetic reaction centers in trehalose glasses: Coupling between protein conformational dynamics and electron-transfer kinetics as studied by laser-flash and high-field EPR spectroscopies
    • A. Savitsky, M. Malferrari, F. Francia, G. Venturoli, and K. Möbius Bacterial photosynthetic reaction centers in trehalose glasses: coupling between protein conformational dynamics and electron-transfer kinetics as studied by laser-flash and high-field EPR spectroscopies J. Phys. Chem. B 114 2010 12729 12743
    • (2010) J. Phys. Chem. B , vol.114 , pp. 12729-12743
    • Savitsky, A.1    Malferrari, M.2    Francia, F.3    Venturoli, G.4    Möbius, K.5
  • 26
    • 0002859824 scopus 로고    scopus 로고
    • Light-induced Fourier transform infrared difference spectroscopy of the primary electron donor in photosynthetic reaction centers
    • H.H. Mantsch, D. Chapman, Wiley-Liss New York
    • E. Nabedryk Light-induced Fourier transform infrared difference spectroscopy of the primary electron donor in photosynthetic reaction centers H.H. Mantsch, D. Chapman, Infrared Spectroscopy of Biomolecules 1996 Wiley-Liss New York 39 82
    • (1996) Infrared Spectroscopy of Biomolecules , pp. 39-82
    • Nabedryk, E.1
  • 27
    • 26444511079 scopus 로고    scopus 로고
    • Investigation of ubiquinol formation in isolated photosynthetic reaction centers by rapid-scan Fourier transform IR spectroscopy
    • A. Mezzetti, and W. Leibl Investigation of ubiquinol formation in isolated photosynthetic reaction centers by rapid-scan Fourier transform IR spectroscopy Eur. Biophys. J. 34 2005 921 936
    • (2005) Eur. Biophys. J. , vol.34 , pp. 921-936
    • Mezzetti, A.1    Leibl, W.2
  • 28
    • 33751242792 scopus 로고    scopus 로고
    • Proton uptake in the reaction center mutant L210DN from Rhodobacter sphaeroides via protonated water molecules
    • S. Hermes, J.M. Stachnik, D. Onidas, A. Remy, E. Hofmann, and K. Gerwert Proton uptake in the reaction center mutant L210DN from Rhodobacter sphaeroides via protonated water molecules Biochemistry 45 2006 13741 13749
    • (2006) Biochemistry , vol.45 , pp. 13741-13749
    • Hermes, S.1    Stachnik, J.M.2    Onidas, D.3    Remy, A.4    Hofmann, E.5    Gerwert, K.6
  • 29
    • 52949129815 scopus 로고    scopus 로고
    • B site of the bacterial reaction center: A perspective from FTIR difference spectroscopy
    • B site of the bacterial reaction center: a perspective from FTIR difference spectroscopy Biochim. Biophys. Acta 1777 2008 1229 1248
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1229-1248
    • Nabedryk, E.1    Breton, J.2
  • 32
    • 84985164554 scopus 로고
    • Oxidation-reduction physical chemistry of the acceptor quinone complex in bacterial photosynthetic reaction centers: Evidence for a new model of herbicide activity
    • C.A. Wraight Oxidation-reduction physical chemistry of the acceptor quinone complex in bacterial photosynthetic reaction centers: evidence for a new model of herbicide activity Isr. J. Chem. 21 1981 348 354
    • (1981) Isr. J. Chem. , vol.21 , pp. 348-354
    • Wraight, C.A.1
  • 34
    • 0026051114 scopus 로고
    • Probing the primary quinone environment in photosynthetic bacterial reaction centers by light-induced FTIR difference spectroscopy
    • J. Breton, D.L. Thibodeau, C. Berthomieu, W. Mäntele, A. Verméglio, and E. Nabedryk Probing the primary quinone environment in photosynthetic bacterial reaction centers by light-induced FTIR difference spectroscopy FEBS Lett. 278 1991 257 260
    • (1991) FEBS Lett. , vol.278 , pp. 257-260
    • Breton, J.1    Thibodeau, D.L.2    Berthomieu, C.3    Mäntele, W.4    Verméglio, A.5    Nabedryk, E.6
  • 35
    • 0015514066 scopus 로고
    • Electron acceptors in reaction center preparations from photosynthetic bacteria
    • L. Sloten Electron acceptors in reaction center preparations from photosynthetic bacteria Biochim. Biophys. Acta 275 1972 208 218
    • (1972) Biochim. Biophys. Acta , vol.275 , pp. 208-218
    • Sloten, L.1
  • 36
    • 0031234145 scopus 로고    scopus 로고
    • Binding of ubiquinone to photosynthetic reaction centers: Determination of enthalpy and entropy changes in reverse micelles
    • A. Mallardi, G. Palazzo, and G. Venturoli Binding of ubiquinone to photosynthetic reaction centers: determination of enthalpy and entropy changes in reverse micelles J. Phys. Chem. B 101 1997 7850 7857
    • (1997) J. Phys. Chem. B , vol.101 , pp. 7850-7857
    • Mallardi, A.1    Palazzo, G.2    Venturoli, G.3
  • 38
    • 0035992560 scopus 로고    scopus 로고
    • Attenuate total reflection Fourier transform infrared spectroscopy of redox transition in photosynthetic reaction centers: Comparison of perfusion- and light-induced difference spectra
    • M. Iwaki, S. Andrianambinintsoa, P. Rich, and J. Breton Attenuate total reflection Fourier transform infrared spectroscopy of redox transition in photosynthetic reaction centers: comparison of perfusion- and light-induced difference spectra Spectrochim. Acta Part A 58 2002 1523 1533
    • (2002) Spectrochim. Acta Part A , vol.58 , pp. 1523-1533
    • Iwaki, M.1    Andrianambinintsoa, S.2    Rich, P.3    Breton, J.4
  • 39
    • 0034191812 scopus 로고    scopus 로고
    • Heteromeric versus homodimeric structure of the primary electron donor in Rhodobacter sphaeroides reaction centers genetically modified at position M202
    • E. Nabedryk, C. Schulz, F. Müh, W. Lubitz, and J. Breton Heteromeric versus homodimeric structure of the primary electron donor in Rhodobacter sphaeroides reaction centers genetically modified at position M202 Photochem. Photobiol. 71 2000 582 588
    • (2000) Photochem. Photobiol. , vol.71 , pp. 582-588
    • Nabedryk, E.1    Schulz, C.2    Müh, F.3    Lubitz, W.4    Breton, J.5
  • 40
    • 0026787637 scopus 로고
    • A new infrared electronic transition of the oxidized primary electron donor in bacterial reaction centers: A way to assess resonance interactions between the bacteriochlorophylls
    • J. Breton, E. Nabedryk, and W.W. Parson A new infrared electronic transition of the oxidized primary electron donor in bacterial reaction centers: a way to assess resonance interactions between the bacteriochlorophylls Biochemistry 31 1992 7503 7510
    • (1992) Biochemistry , vol.31 , pp. 7503-7510
    • Breton, J.1    Nabedryk, E.2    Parson, W.W.3
  • 42
    • 0031858264 scopus 로고    scopus 로고
    • Proton uptake upon quinone reduction in bacterial reaction centers: IR signature and possible participation of a highly polarisable hydrogen bond network
    • J. Breton, and E. Nabedryk Proton uptake upon quinone reduction in bacterial reaction centers: IR signature and possible participation of a highly polarisable hydrogen bond network Photosynth. Res. 55 1998 301 307
    • (1998) Photosynth. Res. , vol.55 , pp. 301-307
    • Breton, J.1    Nabedryk, E.2
  • 43
    • 0033524430 scopus 로고    scopus 로고
    • A and a histidine side chain in photosystem II as revealed by Fourier transform infrared spectroscopy
    • A and a histidine side chain in photosystem II as revealed by Fourier transform infrared spectroscopy Biochemistry 38 1999 399 403
    • (1999) Biochemistry , vol.38 , pp. 399-403
    • Noguchi, T.1    Inoue, Y.2    Tang, X.S.3
  • 44
    • 82755181814 scopus 로고    scopus 로고
    • Charge separation in photosystem II: A comparative and evolutionary overview
    • T. Cardona, A. Sedoud, N. Cox, and A.W. Rutherford Charge separation in photosystem II: a comparative and evolutionary overview Biochim. Biophys. Acta 1817 2012 26 43
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 26-43
    • Cardona, T.1    Sedoud, A.2    Cox, N.3    Rutherford, A.W.4
  • 45
    • 78149409234 scopus 로고    scopus 로고
    • Histidine is involved in coupling proton uptake to electron transfer in photosynthetic proteins
    • D. Onidas, J.M. Stachnik, S. Brucker, S. Krätzig, and K. Gerwert Histidine is involved in coupling proton uptake to electron transfer in photosynthetic proteins Eur. J. Cell Biol. 89 2010 983 989
    • (2010) Eur. J. Cell Biol. , vol.89 , pp. 983-989
    • Onidas, D.1    Stachnik, J.M.2    Brucker, S.3    Krätzig, S.4    Gerwert, K.5
  • 46
    • 41449088527 scopus 로고    scopus 로고
    • Active internal waters in the bacteriorhodopsin photocycle. A comparative study of the L and M intermediates at room and cryogenic temperatures by infrared spectroscopy
    • V.A. Lórenz-Fonfría, Y. Furutani, and H. Kandori Active internal waters in the bacteriorhodopsin photocycle. A comparative study of the L and M intermediates at room and cryogenic temperatures by infrared spectroscopy Biochemistry 47 2008 4071 4081
    • (2008) Biochemistry , vol.47 , pp. 4071-4081
    • Lórenz-Fonfría, V.A.1    Furutani, Y.2    Kandori, H.3
  • 47
    • 0037133143 scopus 로고    scopus 로고
    • Flash-induced FTIR difference spectra of the water oxidizing complex in moderately hydrated photosystem II core films: Effect of hydration extent on S-state transitions
    • T. Noguchi, and M. Sugiura Flash-induced FTIR difference spectra of the water oxidizing complex in moderately hydrated photosystem II core films: effect of hydration extent on S-state transitions Biochemistry 41 2002 2322 2330
    • (2002) Biochemistry , vol.41 , pp. 2322-2330
    • Noguchi, T.1    Sugiura, M.2
  • 48
    • 79957707195 scopus 로고    scopus 로고
    • Water molecule organization in cytochrome c oxidase revealed by FTIR spectroscopy
    • A. Maréchal, and P. Rich Water molecule organization in cytochrome c oxidase revealed by FTIR spectroscopy Proc. Natl. Acad. Sci. U. S. A. 108 2011 8634 8638
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 8634-8638
    • Maréchal, A.1    Rich, P.2
  • 50
    • 0034734254 scopus 로고    scopus 로고
    • Role of internal water molecules in bacteriorhodopsin
    • H. Kandori Role of internal water molecules in bacteriorhodopsin Biochim. Biophys. Acta 1460 2000 177 191
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 177-191
    • Kandori, H.1
  • 51
    • 0000474055 scopus 로고
    • The near infra-red spectrum of the peptide group
    • K.T. Hecht, and D.L. Wood The near infra-red spectrum of the peptide group Proc. R. Soc. Lond. Ser. A 235 1956 174 188
    • (1956) Proc. R. Soc. Lond. Ser. A , vol.235 , pp. 174-188
    • Hecht, K.T.1    Wood, D.L.2
  • 52
    • 0034636790 scopus 로고    scopus 로고
    • Water structural changes involved in the activation process of photoactive yellow protein
    • H. Kandori, T. Iwata, J. Hendriks, A. Maeda, and K.J. Hellingwerf Water structural changes involved in the activation process of photoactive yellow protein Biochemistry 39 2000 7902 7909
    • (2000) Biochemistry , vol.39 , pp. 7902-7909
    • Kandori, H.1    Iwata, T.2    Hendriks, J.3    Maeda, A.4    Hellingwerf, K.J.5
  • 53
    • 38049004891 scopus 로고    scopus 로고
    • Fourier transform infrared analysis of the photosynthetic oxygen-evolving center
    • T. Noguchi Fourier transform infrared analysis of the photosynthetic oxygen-evolving center Coord. Chem. Rev. 252 2008 336 346
    • (2008) Coord. Chem. Rev. , vol.252 , pp. 336-346
    • Noguchi, T.1
  • 54
    • 0027762031 scopus 로고
    • Fourier transform infrared study of the primary electron donor in chromatophores of Rhodobacter sphaeroides with reaction centers genetically modified at residues M160 and L131
    • E. Nabedryk, J.P. Allen, A.K.W. Tagichi, J.C. Williams, N.W. Woodbury, and J. Breton Fourier transform infrared study of the primary electron donor in chromatophores of Rhodobacter sphaeroides with reaction centers genetically modified at residues M160 and L131 Biochemistry 32 1993 13879 13885
    • (1993) Biochemistry , vol.32 , pp. 13879-13885
    • Nabedryk, E.1    Allen, J.P.2    Tagichi, A.K.W.3    Williams, J.C.4    Woodbury, N.W.5    Breton, J.6
  • 56
    • 0033849948 scopus 로고    scopus 로고
    • Self-regulation phenomena in bacterial reaction centers. I. General theory
    • A.O. Goushcha, V.N. Kharkyanen, G.W. Scott, and A.R. Holzwarth Self-regulation phenomena in bacterial reaction centers. I. General theory Biophys. J. 79 2000 1237 1252
    • (2000) Biophys. J. , vol.79 , pp. 1237-1252
    • Goushcha, A.O.1    Kharkyanen, V.N.2    Scott, G.W.3    Holzwarth, A.R.4
  • 58
    • 0036534542 scopus 로고    scopus 로고
    • Protein-water interactions in a dynamic world
    • C. Mattos Protein-water interactions in a dynamic world Trends Biochem. Sci. 27 2002 203 208
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 203-208
    • Mattos, C.1
  • 61
    • 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, A.R. Klingen, P. Sebban, G.M. Ullmann, and G. Fritzsch pH modulates the quinone position in the photosynthetic reaction center from Rhodobacter sphaeroides in the neutral and charge separated states J. Mol. Biol. 371 2007 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
  • 62
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction center from Rhodobacter sphaeroides at 2.65 Å resolution. Cofactors and protein-cofactor interactions
    • U. Ermler, G. Frtzsch, S.K. Buchanan, and H. Michel Structure of the photosynthetic reaction center from Rhodobacter sphaeroides at 2.65 Å resolution. Cofactors and protein-cofactor interactions Structure 2 1994 925 936
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Frtzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 63
    • 0031875589 scopus 로고    scopus 로고
    • Water clusters in the reaction centre of Rhodobacter spaheroides
    • G. Fritzsch, L. Kampmann, G. Kapaun, and H. Michel Water clusters in the reaction centre of Rhodobacter spaheroides Photosynth. Res. 55 1998 127 132
    • (1998) Photosynth. Res. , vol.55 , pp. 127-132
    • Fritzsch, G.1    Kampmann, L.2    Kapaun, G.3    Michel, H.4
  • 65
    • 70350074909 scopus 로고    scopus 로고
    • Lipidic sponge phase crystal structure of a photosynthetic reaction center reveals lipids on the protein surface
    • A.B. Wöhri, W.Y. Wahlgren, E. Malmerberg, L.C. Johansson, R. Neutze, and G. Katona Lipidic sponge phase crystal structure of a photosynthetic reaction center reveals lipids on the protein surface Biochemistry 48 2009 9831 9838
    • (2009) Biochemistry , vol.48 , pp. 9831-9838
    • Wöhri, A.B.1    Wahlgren, W.Y.2    Malmerberg, E.3    Johansson, L.C.4    Neutze, R.5    Katona, G.6


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