메뉴 건너뛰기




Volumn 96, Issue 12, 2009, Pages 4956-4965

Identification of the intermediate charge-separated state P +βL- in a leucine M214 to histidine mutant of the Rhodobacter sphaeroides reaction center using femtosecond midinfrared spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOCHLOROPHYLL; BACTERIOPHEOPHYTIN; CARBONYL DERIVATIVE; HISTIDINE; LEUCINE;

EID: 68949083188     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.03.031     Document Type: Article
Times cited : (5)

References (41)
  • 1
    • 51049111660 scopus 로고    scopus 로고
    • Identification of the first steps in charge separation in bacterial photosynthetic reaction centers of Rhodobacter sphaeroides by ultrafast mid-infrared spectroscopy: Electron transfer and protein dynamics
    • Pawlowicz, N. P., R. van Grondelle, I. H. M. van Stokkum, J. Breton, M. R. Jones, et al. 2008. Identification of the first steps in charge separation in bacterial photosynthetic reaction centers of Rhodobacter sphaeroides by ultrafast mid-infrared spectroscopy: electron transfer and protein dynamics. Biophys. J. 95:1268-1284.
    • (2008) Biophys. J , vol.95 , pp. 1268-1284
    • Pawlowicz, N.P.1    van Grondelle, R.2    van Stokkum, I.H.M.3    Breton, J.4    Jones, M.R.5
  • 2
    • 68949156068 scopus 로고    scopus 로고
    • Charge separation in tyrosine M210 to tryptophan mutant of the Rhodobacter sphaeroides reaction center studied with femtosecond mid-infrared spectroscopy
    • Submitted
    • Pawlowicz, N. P., I. H. M. van Stokkum, J. Breton, R. van Grondelle, and M. R. Jones. 2008. Charge separation in tyrosine M210 to tryptophan mutant of the Rhodobacter sphaeroides reaction center studied with femtosecond mid-infrared spectroscopy. Phys. Chem. Chem. Phys. Submitted.
    • (2008) Phys. Chem. Chem. Phys
    • Pawlowicz, N.P.1    van Stokkum, I.H.M.2    Breton, J.3    van Grondelle, R.4    Jones, M.R.5
  • 3
    • 68949156951 scopus 로고    scopus 로고
    • Multi-phasic radical pair relaxation in bacterial reaction centers that lack the primary quinone studied by femtosecond visible pump/mid-IR probe spectroscopy
    • Submitted
    • Pawlowicz, N. P., I. H. M. van Stokkum, J. Breton, R. van Grondelle, and M. R. Jones. 2008. Multi-phasic radical pair relaxation in bacterial reaction centers that lack the primary quinone studied by femtosecond visible pump/mid-IR probe spectroscopy. Photosynth. Res. Submitted.
    • (2008) Photosynth. Res
    • Pawlowicz, N.P.1    van Stokkum, I.H.M.2    Breton, J.3    van Grondelle, R.4    Jones, M.R.5
  • 4
    • 0025907020 scopus 로고
    • Charge separation in a reaction center incorporating bacteriochlorophyll for photoactive bacteriopheophytin
    • Kirmaier, C., D. Gaul, R. DeBey, D. Holten, and C. C. Schenck. 1991. Charge separation in a reaction center incorporating bacteriochlorophyll for photoactive bacteriopheophytin. Science. 251:922-927.
    • (1991) Science , vol.251 , pp. 922-927
    • Kirmaier, C.1    Gaul, D.2    DeBey, R.3    Holten, D.4    Schenck, C.C.5
  • 5
    • 0024110444 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1 - protein-cofactor (bacteriochlorophyll, bacteriopheophytin and carotenoid) interactions
    • Yeates, T. O., H. Komiya, A. Chirino, D. C. Rees, J. P. Allen, et al. 1988. Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1 - protein-cofactor (bacteriochlorophyll, bacteriopheophytin and carotenoid) interactions. Proc. Natl. Acad. Sci. USA. 85:7993-7997.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7993-7997
    • Yeates, T.O.1    Komiya, H.2    Chirino, A.3    Rees, D.C.4    Allen, J.P.5
  • 6
    • 0024157070 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1 - symmetry relations and sequence comparisons between different species
    • Komiya, H., T. O. Yeates, D. C. Rees, J. P. Allen, and G. Feher. 1988. Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1 - symmetry relations and sequence comparisons between different species. Proc. Natl. Acad. Sci. USA. 85:9012-9016.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9012-9016
    • Komiya, H.1    Yeates, T.O.2    Rees, D.C.3    Allen, J.P.4    Feher, G.5
  • 7
    • 0028281478 scopus 로고
    • Crystallographic analyses of site-directed mutants of the photosynthetic reaction center from Rhodobacter sphaeroides
    • Chirino, A. J., E. J. Lous, M. Huber, J. P. Allen, C. C. Schenck, et al. 1994. Crystallographic analyses of site-directed mutants of the photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry. 33:4584-4593.
    • (1994) Biochemistry , vol.33 , pp. 4584-4593
    • Chirino, A.J.1    Lous, E.J.2    Huber, M.3    Allen, J.P.4    Schenck, C.C.5
  • 8
    • 18244409359 scopus 로고    scopus 로고
    • B) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: Quantum efficiency and X-ray structure
    • B) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: quantum efficiency and X-ray structure. Biochemistry. 44:6920-6928.
    • (2005) Biochemistry , vol.44 , pp. 6920-6928
    • Paddock, M.L.1    Chang, C.2    Xu, Q.3    Abresch, E.C.4    Axelrod, H.L.5
  • 9
    • 0029305402 scopus 로고
    • The nature and dynamics of the charge-separated intermediate in reaction centers in which bacteriochlorophyll replaces the photoactive bacteriopheophytin. 1. Spectral characterization of the transient state
    • Kirmaier, C., L. Laporte, C. C. Schenck, and D. Holten. 1995. The nature and dynamics of the charge-separated intermediate in reaction centers in which bacteriochlorophyll replaces the photoactive bacteriopheophytin. 1. Spectral characterization of the transient state. J. Phys. Chem. 99:8903-8909.
    • (1995) J. Phys. Chem , vol.99 , pp. 8903-8909
    • Kirmaier, C.1    Laporte, L.2    Schenck, C.C.3    Holten, D.4
  • 10
    • 0029647453 scopus 로고
    • Control of electron transfer between the L- and M-sides of photosynthetic reaction centers
    • Heller, B. A., D. Holten, and C. Kirmaier. 1995. Control of electron transfer between the L- and M-sides of photosynthetic reaction centers. Science. 269:940-945.
    • (1995) Science , vol.269 , pp. 940-945
    • Heller, B.A.1    Holten, D.2    Kirmaier, C.3
  • 11
    • 0029305402 scopus 로고
    • The nature and dynamics of the charge-separated intermediate in reaction centers in which bacteriochlorophyll replaces the photoactive bacteriopheophytin. 2. The rates and yields of charge separation and recombination
    • Kirmaier, C., L. Laporte, C. C. Schenck, and D. Holten. 1995. The nature and dynamics of the charge-separated intermediate in reaction centers in which bacteriochlorophyll replaces the photoactive bacteriopheophytin. 2. The rates and yields of charge separation and recombination. J. Phys. Chem. B. 99:8910-8917.
    • (1995) J. Phys. Chem. B , vol.99 , pp. 8910-8917
    • Kirmaier, C.1    Laporte, L.2    Schenck, C.C.3    Holten, D.4
  • 12
    • 26844443360 scopus 로고    scopus 로고
    • Electron transfer in the reaction center of the Rb. sphaeroides R-26 studied by transient absorption
    • Ziolek, M., N. Pawlowicz, R. Naskrecki, and A. Dobek. 2005. Electron transfer in the reaction center of the Rb. sphaeroides R-26 studied by transient absorption. J. Phys. Chem. B. 109:18171-18176.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 18171-18176
    • Ziolek, M.1    Pawlowicz, N.2    Naskrecki, R.3    Dobek, A.4
  • 13
    • 0029638667 scopus 로고
    • Ultrafast initial reaction in bacterial photosynthesis revealed by femtosecond infrared spectroscopy
    • Hamm, P., and W. Zinth. 1995. Ultrafast initial reaction in bacterial photosynthesis revealed by femtosecond infrared spectroscopy. J. Phys. Chem. 99:13537-13544.
    • (1995) J. Phys. Chem , vol.99 , pp. 13537-13544
    • Hamm, P.1    Zinth, W.2
  • 14
    • 0002210797 scopus 로고
    • Correlation of structural and spectroscopic properties of a photosynthetic reaction center
    • Zinth, W., E. W. Knapp, S. F. Fischer, W. Kaiser, J. Deisenhofer, et al. 1985. Correlation of structural and spectroscopic properties of a photosynthetic reaction center. Chem. Phys. Lett. 119:1-4.
    • (1985) Chem. Phys. Lett , vol.119 , pp. 1-4
    • Zinth, W.1    Knapp, E.W.2    Fischer, S.F.3    Kaiser, W.4    Deisenhofer, J.5
  • 15
    • 0021741695 scopus 로고
    • Nanosecond fluorescence from isolated photosynthetic reaction centers of Rhodopseudomonas sphaeroides
    • Woodbury, N. W. T., and W. W. Parson. 1984. Nanosecond fluorescence from isolated photosynthetic reaction centers of Rhodopseudomonas sphaeroides. Biochim. Biophys. Acta. 767:345-361.
    • (1984) Biochim. Biophys. Acta , vol.767 , pp. 345-361
    • Woodbury, N.W.T.1    Parson, W.W.2
  • 16
    • 0001337010 scopus 로고
    • The pathway, kinetics and thermodynamics of electron transfer in wild type and mutant bacterial reaction centers of purple nonsulfur bacteria
    • Bacteria. R. E. Blankenship, M. T. Madigan, and C. E. Bauer, editors. Kluwer Academic, Dordrecht, The Netherlands
    • Woodbury, N. W., and J. P. Allen. 1995. The pathway, kinetics and thermodynamics of electron transfer in wild type and mutant bacterial reaction centers of purple nonsulfur bacteria. In Anoxygenic Photosynthetic Bacteria. R. E. Blankenship, M. T. Madigan, and C. E. Bauer, editors. Kluwer Academic, Dordrecht, The Netherlands. 527-557.
    • (1995) Anoxygenic Photosynthetic , pp. 527-557
    • Woodbury, N.W.1    Allen, J.P.2
  • 17
    • 0002621519 scopus 로고
    • Radicalpair decay kinetics, triplet yields and delayed fluorescence from bacterial reaction centers
    • Schenck, C. C., R. E. Blankenship, and W. W. Parson. 1982. Radicalpair decay kinetics, triplet yields and delayed fluorescence from bacterial reaction centers. Biochim. Biophys. Acta. 680:44-59.
    • (1982) Biochim. Biophys. Acta , vol.680 , pp. 44-59
    • Schenck, C.C.1    Blankenship, R.E.2    Parson, W.W.3
  • 18
    • 0024355943 scopus 로고
    • A superexchange mechanism for the primary charge separation in photosynthetic reaction centers
    • Bixon, M., J. Jortner, M. E. Michel-Beyerle, and A. Ogrodnik. 1989. A superexchange mechanism for the primary charge separation in photosynthetic reaction centers. Biochim. Biophys. Acta. 977:273-286.
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 273-286
    • Bixon, M.1    Jortner, J.2    Michel-Beyerle, M.E.3    Ogrodnik, A.4
  • 19
    • 0024433957 scopus 로고
    • The effect of very high magnetic fields on the reaction dynamics in bacterial reaction centers - implications for the reaction mechanism
    • Goldstein, R. A., and S. G. Boxer. 1989. The effect of very high magnetic fields on the reaction dynamics in bacterial reaction centers - implications for the reaction mechanism. Biochim. Biophys. Acta. 977:78-86.
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 78-86
    • Goldstein, R.A.1    Boxer, S.G.2
  • 20
    • 0042825748 scopus 로고    scopus 로고
    • Initial steps of signal generation in photoactive yellow protein revealed with femtosecond mid-infrared spectroscopy
    • Groot, M. L., L. J. G. W. van Wilderen, D. S. Larsen, M. A. van der Horst, I. H. M. van Stokkum, et al. 2003. Initial steps of signal generation in photoactive yellow protein revealed with femtosecond mid-infrared spectroscopy. Biochemistry. 42:10054-10059.
    • (2003) Biochemistry , vol.42 , pp. 10054-10059
    • Groot, M.L.1    van Wilderen, L.J.G.W.2    Larsen, D.S.3    van der Horst, M.A.4    van Stokkum, I.H.M.5
  • 21
    • 3042642769 scopus 로고    scopus 로고
    • Femtosecond visible/visible and visible/ mid-IR pump-probe study of the Photosystem II core antenna complex CP47
    • Groot, M. L., J. Breton, L. J. G. W. van Wilderen, J. P. Dekker, and R. van Grondelle. 2004. Femtosecond visible/visible and visible/ mid-IR pump-probe study of the Photosystem II core antenna complex CP47. J. Phys. Chem. B. 108:8001-8006.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 8001-8006
    • Groot, M.L.1    Breton, J.2    van Wilderen, L.J.G.W.3    Dekker, J.P.4    van Grondelle, R.5
  • 23
    • 0032492681 scopus 로고    scopus 로고
    • Structural studies of wild type and mutant reaction centers from an antenna-deficient strain of Rhodobacter sphaeroides: Monitoring the optical properties of the complex from bacterial cell to crystal
    • McAuley-Hecht, K. E., P. K. Fyfe, J. P. Ridge, S. M. Prince, C. N. Hunter, et al. 1998. Structural studies of wild type and mutant reaction centers from an antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical properties of the complex from bacterial cell to crystal. Biochemistry. 37:4740-4750.
    • (1998) Biochemistry , vol.37 , pp. 4740-4750
    • McAuley-Hecht, K.E.1    Fyfe, P.K.2    Ridge, J.P.3    Prince, S.M.4    Hunter, C.N.5
  • 24
    • 0030984493 scopus 로고    scopus 로고
    • Primary electron transfer kinetics in membrane-bound Rhodobacter sphaeroides reaction centers: A global and target analysis
    • van Stokkum, I. H. M., L. M. P. Beekman, M. R. Jones, M. E. van Brederode, and R. van Grondelle. 1997. Primary electron transfer kinetics in membrane-bound Rhodobacter sphaeroides reaction centers: a global and target analysis. Biochemistry. 36:11360-11368.
    • (1997) Biochemistry , vol.36 , pp. 11360-11368
    • van Stokkum, I.H.M.1    Beekman, L.M.P.2    Jones, M.R.3    van Brederode, M.E.4    van Grondelle, R.5
  • 26
  • 27
    • 17344374476 scopus 로고    scopus 로고
    • Excitonic free induction decay studied with femtosecond pulse pairs
    • Mitsumori, Y., H. Fukushima, M. Ogura, T. Kuroda, S. Koshihara, et al. 1996. Excitonic free induction decay studied with femtosecond pulse pairs. J. Lumin. 66&67:81-83.
    • (1996) J. Lumin , vol.66-67 , pp. 81-83
    • Mitsumori, Y.1    Fukushima, H.2    Ogura, M.3    Kuroda, T.4    Koshihara, S.5
  • 28
    • 0025292657 scopus 로고
    • A protein conformational change associated with the photoreduction of the primary and secondary quinones in the bacterial reaction center
    • Nabedryk, E., K. A. Bagley, D. L. Thibodeau, M. Bauscher, W. Mantele, et al. 1990. A protein conformational change associated with the photoreduction of the primary and secondary quinones in the bacterial reaction center. FEBS Lett. 266:59-62.
    • (1990) FEBS Lett , vol.266 , pp. 59-62
    • Nabedryk, E.1    Bagley, K.A.2    Thibodeau, D.L.3    Bauscher, M.4    Mantele, W.5
  • 29
    • 0026051114 scopus 로고
    • Probing the primary quinone environment in photosynthetic bacterial reaction centers by light-induced FTIR difference spectroscopy
    • Breton, J., D. L. Thibodeau, C. Berthomieu, W. Mantele, A. Vermeglio, et al. 1991. Probing the primary quinone environment in photosynthetic bacterial reaction centers by light-induced FTIR difference spectroscopy. FEBS Lett. 278:257-260.
    • (1991) FEBS Lett , vol.278 , pp. 257-260
    • Breton, J.1    Thibodeau, D.L.2    Berthomieu, C.3    Mantele, W.4    Vermeglio, A.5
  • 30
    • 85031366138 scopus 로고    scopus 로고
    • - states in reaction centers from Rb. sphaeroides. In Current Research in Photosynthesis. M. Baltscheffsky, editor. Kluwer Academic Publishers, Dordrecht, The Netherlands. 77-80.
    • - states in reaction centers from Rb. sphaeroides. In Current Research in Photosynthesis. M. Baltscheffsky, editor. Kluwer Academic Publishers, Dordrecht, The Netherlands. 77-80.
  • 31
    • 0002859824 scopus 로고    scopus 로고
    • Light-induced Fourier transform infrared difference spectroscopy of the primary electron donor in photosynthetic reaction centers
    • H. H. Mantsch and D. Chapman, editors. Wiley-Liss, New York
    • Nabedryk, E. 1996. Light-induced Fourier transform infrared difference spectroscopy of the primary electron donor in photosynthetic reaction centers. In Infrared Spectroscopy of Biomolecules. H. H. Mantsch and D. Chapman, editors. Wiley-Liss, New York. 39-81.
    • (1996) Infrared Spectroscopy of Biomolecules , pp. 39-81
    • Nabedryk, E.1
  • 32
    • 0027213057 scopus 로고
    • Electron transfer in pheophytin a-modified reaction centers from Rhodobacter sphaeroides (R-26)
    • Shkuropatov, A. Y., and V. A. Shuvalov. 1993. Electron transfer in pheophytin a-modified reaction centers from Rhodobacter sphaeroides (R-26). FEBS Lett. 322:168-172.
    • (1993) FEBS Lett , vol.322 , pp. 168-172
    • Shkuropatov, A.Y.1    Shuvalov, V.A.2
  • 34
    • 0030592169 scopus 로고    scopus 로고
    • Protein-quinone interactions in the bacterial photosynthetic reaction center: Light-induced FTIR difference spectroscopy of the quinone vibrations
    • Breton, J., and E. Nabedryk. 1996. Protein-quinone interactions in the bacterial photosynthetic reaction center: light-induced FTIR difference spectroscopy of the quinone vibrations. Biochim. Biophys. Acta Bioenerg. 1275:84-90.
    • (1996) Biochim. Biophys. Acta Bioenerg , vol.1275 , pp. 84-90
    • Breton, J.1    Nabedryk, E.2
  • 35
    • 0002939613 scopus 로고
    • FTIR difference spectroscopy of mena-quinone photo-reduction in bacterial reaction centers
    • Molecules R. E. Hester and R. B. Girling, editors. The Royal Society of Chemistry, Cambridge, UK
    • Breton, J., M. Bauscher, C. Berthomieu, D. L. Thibodeau, S. Andiranambinintsoa, D. Dejonghe, W. Mantele, and E. Nabedryk. 1991. FTIR difference spectroscopy of mena-quinone photo-reduction in bacterial reaction centers. In Spectroscopy of Biological Molecules R. E. Hester and R. B. Girling, editors. The Royal Society of Chemistry, Cambridge, UK. 43-46.
    • (1991) Spectroscopy of Biological , pp. 43-46
    • Breton, J.1    Bauscher, M.2    Berthomieu, C.3    Thibodeau, D.L.4    Andiranambinintsoa, S.5    Dejonghe, D.6    Mantele, W.7    Nabedryk, E.8
  • 36
    • 0030612688 scopus 로고    scopus 로고
    • A demonstrated by mutations at residues Glu L104 and Trp L100 in reaction centers from Rhodobacter sphaeroides
    • A demonstrated by mutations at residues Glu L104 and Trp L100 in reaction centers from Rhodobacter sphaeroides. Biochemistry. 36:4515-4525.
    • (1997) Biochemistry , vol.36 , pp. 4515-4525
    • Breton, J.1    Nabedryk, E.2    Allen, J.P.3    Williams, J.C.4
  • 37
    • 0000627943 scopus 로고
    • Infrared spectroelectrochemistry of bacteriochlorophylls and bacteriopheophytins - implications for the binding of the pigments in the reaction center from photosynthetic bacteria
    • Mantele, W. G., A. M. Wollenweber, E. Nabedryk, and J. Breton. 1988. Infrared spectroelectrochemistry of bacteriochlorophylls and bacteriopheophytins - implications for the binding of the pigments in the reaction center from photosynthetic bacteria. Proc. Natl. Acad. Sci. USA. 85:8468-8472.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8468-8472
    • Mantele, W.G.1    Wollenweber, A.M.2    Nabedryk, E.3    Breton, J.4
  • 38
    • 21844515600 scopus 로고
    • FTIR Spectroscopy of the photoreduction of the bacteriopheophytin electron acceptor in reaction centers of Rhodobacter sphaeroides and Rhodopseudomonas viridis
    • Nabedryk, E., S. Andrianambinintsoa, D. Dejonghe, and J. Breton. 1995. FTIR Spectroscopy of the photoreduction of the bacteriopheophytin electron acceptor in reaction centers of Rhodobacter sphaeroides and Rhodopseudomonas viridis. Chem. Phys. 194:371-378.
    • (1995) Chem. Phys , vol.194 , pp. 371-378
    • Nabedryk, E.1    Andrianambinintsoa, S.2    Dejonghe, D.3    Breton, J.4
  • 39
    • 0027288334 scopus 로고
    • Picosecond infrared studies of the dynamics of the photosynthetic reaction center
    • Maiti, S., B. R. Cowen, R. Diller, M. Iannone, C. C. Moser, et al. 1993. Picosecond infrared studies of the dynamics of the photosynthetic reaction center. Proc. Natl. Acad. Sci. USA. 90:5247-5251.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5247-5251
    • Maiti, S.1    Cowen, B.R.2    Diller, R.3    Iannone, M.4    Moser, C.C.5
  • 40
    • 0027948980 scopus 로고
    • Femtosecond coherent transient infrared spectroscopy of reaction centers from Rhodobacter sphaeroides
    • Maiti, S., G. C. Walker, B. R. Cowen, R. Pippenger, C. C. Moser, et al. 1994. Femtosecond coherent transient infrared spectroscopy of reaction centers from Rhodobacter sphaeroides. Proc. Natl. Acad. Sci. USA. 91:10360-10364.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10360-10364
    • Maiti, S.1    Walker, G.C.2    Cowen, B.R.3    Pippenger, R.4    Moser, C.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.