메뉴 건너뛰기




Volumn 42, Issue 6, 2003, Pages 1718-1730

Quinone reduction via secondary B-branch electron transfer in mutant bacterial reaction centers

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CHARGE TRANSFER; DETERGENTS; PHOTOSYNTHESIS; REDUCTION;

EID: 0037452511     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026959b     Document Type: Article
Times cited : (62)

References (92)
  • 1
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction center from Rhodopseudomonas viridis at 3 Å resolution
    • Deisenhofer, J., Epp, O., Miki, K., Huber, R., and Michel, H. (1985) Structure of the protein subunits in the photosynthetic reaction center from Rhodopseudomonas viridis at 3 Å resolution, Nature 318, 618-624.
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 2
    • 0023395661 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The cofactors
    • Allen, J. P., Feher, G., Yeates, T. O., Komiya, H., and Rees, D. C. (1987) Structure of the reaction center from Rhodobacter sphaeroides R-26: The cofactors, Proc. Natl. Acad. Sci. U.S.A. 84, 5730-5734.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 5730-5734
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 3
    • 0025784505 scopus 로고
    • The structure of the membrane-bound photosynthetic reaction center from Rhodobacter sphaeroides
    • Chang, C.-H., El-Kabbani, O., Tiede, D. M., Norris, J. R., and Schiffer, M. (1991) The structure of the membrane-bound photosynthetic reaction center from Rhodobacter sphaeroides, Biochemistry 30, 5352-5360.
    • (1991) Biochemistry , vol.30 , pp. 5352-5360
    • Chang, C.-H.1    El-Kabbani, O.2    Tiede, D.M.3    Norris, J.R.4    Schiffer, M.5
  • 4
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactor and protein - Cofactor interactions
    • Ermler, U., Fritsch, G., Buchanan, S. K., and Michel, H. (1994) Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: cofactor and protein - cofactor interactions, Structure 2, 925-936.
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 5
    • 0001337010 scopus 로고
    • The pathway, kinetics, and thermodynamics of electron transfer in wild type and mutant reaction centers of purple nonsulfur bacteria
    • Blankenship, R. E., Madigan, M. T., and Bauer, C. E., Eds., Kluwer, The Netherlands
    • Woodbury, N. W., and Allen, J. P. (1995) The pathway, kinetics, and thermodynamics of electron transfer in wild type and mutant reaction centers of purple nonsulfur bacteria, In Anoxygenic Photosynthetic Bacteria (Blankenship, R. E., Madigan, M. T., and Bauer, C. E., Eds.) pp 527-557, Kluwer, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 527-557
    • Woodbury, N.W.1    Allen, J.P.2
  • 6
    • 0026042671 scopus 로고
    • Kinetic properties of the acceptor quinone complex in Rhodopseudomonas viridis
    • Leibl, W., and Breton, J. (1991) Kinetic properties of the acceptor quinone complex in Rhodopseudomonas viridis, Biochemistry 30, 9634-9642.
    • (1991) Biochemistry , vol.30 , pp. 9634-9642
    • Leibl, W.1    Breton, J.2
  • 7
    • 0029769668 scopus 로고    scopus 로고
    • Time-resolved electrochromism associated with the formation of quinone anions in the Rhodobacter sphaeroides R-26 reaction center
    • Tiede, D. M., Vazquez, J., Cordova, and Marone, P. A. (1996) Time-resolved electrochromism associated with the formation of quinone anions in the Rhodobacter sphaeroides R-26 reaction center, Biochemistry 35, 10763-10775.
    • (1996) Biochemistry , vol.35 , pp. 10763-10775
    • Tiede, D.M.1    Vazquez, J.2    Cordova3    Marone, P.A.4
  • 8
    • 0032478280 scopus 로고    scopus 로고
    • B- and the associated processes in Rhodobacter sphaeroides R-26 reaction centers
    • B- and the associated processes in Rhodobacter sphaeroides R-26 reaction centers, Biochemistry 37, 2818-2829.
    • (1998) Biochemistry , vol.37 , pp. 2818-2829
    • Li, J.1    Gilroy, D.2    Tiede, D.M.3    Gunner, M.R.4
  • 9
    • 0028787627 scopus 로고
    • Electron and proton-transfer to the quinones in bacterial photosynthetic reaction centers - Insight from combined approaches of molecular genetics and biophysics
    • Sebban, P., Maróti, P., and Hanson, D. K. (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
  • 10
    • 0002281681 scopus 로고
    • B in reaction centers from photosynthetic bacteria
    • Blankenship, R. E., Madigan, M. T., and Bauer, C. E., Eds., Kluwer, Dordrecht, The Netherlands
    • B in reaction centers from photosynthetic bacteria, In Anoxygenic Photosynthetic Bacteria (Blankenship, R. E., Madigan, M. T., and Bauer, C. E., Eds.) pp 577-594, Kluwer, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 577-594
    • Okamura, M.Y.1    Feher, G.2
  • 11
    • 12744263523 scopus 로고
    • Primary photochemistry of reaction centers from the photosynthetic purple bacteria
    • Kirmaier, C., and Holten, D. (1987) Primary photochemistry of reaction centers from the photosynthetic purple bacteria, Photosyn. Res. 13, 225-260.
    • (1987) Photosyn. Res. , vol.13 , pp. 225-260
    • Kirmaier, C.1    Holten, D.2
  • 14
    • 0002839430 scopus 로고
    • Measurement of the extent of electron transfer to the bacteriopheophytin in the M-subunit in reaction centers of Rhodopseudomonas viridis
    • Kellogg, E. C., Kolaczkowski, S., Wasielewski, M. R., and Tiede, D. M. (1989) Measurement of the extent of electron transfer to the bacteriopheophytin in the M-subunit in reaction centers of Rhodopseudomonas viridis, Photosyn. Res. 22, 47-59.
    • (1989) Photosyn. Res. , vol.22 , pp. 47-59
    • Kellogg, E.C.1    Kolaczkowski, S.2    Wasielewski, M.R.3    Tiede, D.M.4
  • 15
    • 11644286298 scopus 로고
    • Quantum treatment of the optical spectra and the initial electron-transfer process within the reaction center of Rhodopseudomonas viridis
    • Scherer, P. O. J., and Fischer, S. F. (1989) Quantum treatment of the optical spectra and the initial electron-transfer process within the reaction center of Rhodopseudomonas viridis, Chem. Phys. 131, 115-127.
    • (1989) Chem. Phys. , vol.131 , pp. 115-127
    • Scherer, P.O.J.1    Fischer, S.F.2
  • 16
    • 0025368499 scopus 로고
    • Electrostatic control of charge separation in bacterial photosynthesis
    • Parson, W. W., Chu, Z.-T., and Warshel, A. (1990) Electrostatic control of charge separation in bacterial photosynthesis, Biochim. Biophys. Acta 1017, 251-272.
    • (1990) Biochim. Biophys. Acta , vol.1017 , pp. 251-272
    • Parson, W.W.1    Chu, Z.-T.2    Warshel, A.3
  • 17
    • 0028238239 scopus 로고
    • Dielectric asymmetry in the photosynthetic reaction center
    • Steffen, M. A., Lao, K., and Boxer, S. G. (1994) Dielectric asymmetry in the photosynthetic reaction center, Science 264, 810-816.
    • (1994) Science , vol.264 , pp. 810-816
    • Steffen, M.A.1    Lao, K.2    Boxer, S.G.3
  • 18
    • 0029647453 scopus 로고
    • Control of electron transfer between the L- and M-sides of photosynthetic reaction centers
    • Heller, B. A., Holten, D., and Kirmaier, C. (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
  • 19
    • 0029188718 scopus 로고
    • Calculations of electrostatic energies in photosynthetic reaction centers
    • Alden, R. G., Parson, W. W., Chu, Z. T., and Warshel, A. (1995) Calculations of electrostatic energies in photosynthetic reaction centers, J. Am. Chem. Soc. 117, 12284-12298.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 12284-12298
    • Alden, R.G.1    Parson, W.W.2    Chu, Z.T.3    Warshel, A.4
  • 20
    • 0000414723 scopus 로고    scopus 로고
    • Electrostatic potentials in Rhodopseudomonas viridis reaction centers: Implications for the driving force and directionality of electron transfer
    • Gunner, M. R., Nicholls, A., and Honig, B. (1996) Electrostatic potentials in Rhodopseudomonas viridis reaction centers: implications for the driving force and directionality of electron transfer, J. Phys. Chem. 100, 4277-4291.
    • (1996) J. Phys. Chem. , vol.100 , pp. 4277-4291
    • Gunner, M.R.1    Nicholls, A.2    Honig, B.3
  • 21
  • 22
    • 0000063992 scopus 로고    scopus 로고
    • Ab initio calculation of electronic coupling in the photosynthetic reaction center
    • Zhang, L. Y., and Friesner, R. A. (1998) Ab initio calculation of electronic coupling in the photosynthetic reaction center, Proc. Natl. Acad. Sci. U.S.A. 95, 13603-13605.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13603-13605
    • Zhang, L.Y.1    Friesner, R.A.2
  • 23
    • 0000646009 scopus 로고    scopus 로고
    • Excited states of the photosynthetic reaction center of Rhodopseudomonas viridis: SAC-CI study
    • Hasegawa, J., Ohkawa, K., and Nakatsuji, H. (1998) Excited states of the photosynthetic reaction center of Rhodopseudomonas viridis: SAC-CI study, J. Phys. Chem. B 102, 10410-10419.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 10410-10419
    • Hasegawa, J.1    Ohkawa, K.2    Nakatsuji, H.3
  • 24
    • 0001583619 scopus 로고    scopus 로고
    • B-side electron transfer in a Rhodobacter sphaeroides reaction center mutant in which the B-side monomer bacteriochlorophyll is replaced with bacteriopheophytin
    • Katilius, E., Turanchik, T., Lin, S., Taguchi, A. K. W., and Woodbury, N. W. (1999) B-side electron transfer in a Rhodobacter sphaeroides reaction center mutant in which the B-side monomer bacteriochlorophyll is replaced with bacteriopheophytin, J. Phys. Chem. B 103, 7386-7389.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 7386-7389
    • Katilius, E.1    Turanchik, T.2    Lin, S.3    Taguchi, A.K.W.4    Woodbury, N.W.5
  • 25
    • 0000145470 scopus 로고    scopus 로고
    • Asymmetric electron transfer in reaction centers of purple bacteria strongly depends on different electron matrix elements in the active and inactive branches
    • Kolbasov, D., and Scherz, A. (2000) Asymmetric electron transfer in reaction centers of purple bacteria strongly depends on different electron matrix elements in the active and inactive branches, J. Phys. Chem. B 104, 1802-1809.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 1802-1809
    • Kolbasov, D.1    Scherz, A.2
  • 26
    • 0035833976 scopus 로고    scopus 로고
    • Manipulating the direction of electron transfer in the bacterial reaction center by swapping Phe for Tyr near BChl(M) (L181) and Tyr for Phe near BChI(L) (M208)
    • Kirmaier, C., He, C., and Holten, D. (2001) Manipulating the direction of electron transfer in the bacterial reaction center by swapping Phe for Tyr near BChl(M) (L181) and Tyr for Phe near BChI(L) (M208), Biochemistry 40, 12132-12139.
    • (2001) Biochemistry , vol.40 , pp. 12132-12139
    • Kirmaier, C.1    He, C.2    Holten, D.3
  • 27
    • 0035442638 scopus 로고    scopus 로고
    • Noise breaking the 2-fold symmetry of photosynthetic reaction centers: Electron transfer
    • Pincak, R., and Pudlak, M. (2001) Noise breaking the 2-fold symmetry of photosynthetic reaction centers: Electron transfer, Phys. Rev. E 64, 031906.
    • (2001) Phys. Rev. E , vol.64 , pp. 031906
    • Pincak, R.1    Pudlak, M.2
  • 28
    • 0001583620 scopus 로고    scopus 로고
    • B-side electron-transfer promoted by absorbance of multiple photons in Rhodobacter sphaeroides R-26 reaction centers
    • Lin, S., Jackson, J. A., Taguchi, A. K. W., and Woodbury, N. W. (1999) B-side electron-transfer promoted by absorbance of multiple photons in Rhodobacter sphaeroides R-26 reaction centers, J. Phys. Chem. B 103, 4757-4763.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 4757-4763
    • Lin, S.1    Jackson, J.A.2    Taguchi, A.K.W.3    Woodbury, N.W.4
  • 29
    • 0035923418 scopus 로고    scopus 로고
    • Blue light drives B-side electron transfer in bacterial photosynthetic reaction centers
    • Lin, S., Katilius, E., Haffa, A. L., Taguchi, A. K., and Woodbury, N. W. (2001) Blue light drives B-side electron transfer in bacterial photosynthetic reaction centers, Biochemistry 40, 13767-13773.
    • (2001) Biochemistry , vol.40 , pp. 13767-13773
    • Lin, S.1    Katilius, E.2    Haffa, A.L.3    Taguchi, A.K.4    Woodbury, N.W.5
  • 31
    • 0033621178 scopus 로고    scopus 로고
    • M-side electron transfer in reaction center mutants with a lysine near the nonphotoactive bacteriochlorophyll
    • Kirmaier, C., Weems, D., and Holten, D. (1999) M-side electron transfer in reaction center mutants with a lysine near the nonphotoactive bacteriochlorophyll, Biochemistry 38, 11516-11530.
    • (1999) Biochemistry , vol.38 , pp. 11516-11530
    • Kirmaier, C.1    Weems, D.2    Holten, D.3
  • 32
    • 0037075443 scopus 로고    scopus 로고
    • B-side electron transfer in a Rhodobacter sphaeroides reaction center mutant in which the B side monomer bacteriochlorophyll is replaced with bacteriopheophytin: Low temperature study and energetics of charge-separated states
    • Katilius, E., Katiliene, Z., Lin, S., Taguchi, A. K. W., and Woodbury, N. W. (2002) B-side electron transfer in a Rhodobacter sphaeroides reaction center mutant in which the B side monomer bacteriochlorophyll is replaced with bacteriopheophytin: Low temperature study and energetics of charge-separated states, J. Phys. Chem. B 106, 1471-1475.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 1471-1475
    • Katilius, E.1    Katiliene, Z.2    Lin, S.3    Taguchi, A.K.W.4    Woodbury, N.W.5
  • 34
    • 0037022797 scopus 로고    scopus 로고
    • High yield of B-branch electron transfer in a quadruple reaction center mutant of the photosynthetic bacterium Rhodobacter sphaeroides
    • de Boer, A. L., Neerken, S., de Wijn, R., Permentier, H. P., Gast, P., Vijgenboom, E., and Hoff, A. J. (2002) High yield of B-branch electron transfer in a quadruple reaction center mutant of the photosynthetic bacterium Rhodobacter sphaeroides, Biochemistry 41, 3081-3088.
    • (2002) Biochemistry , vol.41 , pp. 3081-3088
    • De Boer, A.L.1    Neerken, S.2    De Wijn, R.3    Permentier, H.P.4    Gast, P.5    Vijgenboom, E.6    Hoff, A.J.7
  • 35
    • 0036278788 scopus 로고    scopus 로고
    • B-branch electron transfer in reaction centers of Rhodobacter sphaeroides assessed with site-directed mutagenesis
    • de Boer, A. L., Neerken, S., de Wijn, R., Permentier, H. P., Gast, P., Vijgenboom, E., and Hoff, A. J. (2002) B-branch electron transfer in reaction centers of Rhodobacter sphaeroides assessed with site-directed mutagenesis, Photosyn. Res. 71, 221-239.
    • (2002) Photosyn. Res. , vol.71 , pp. 221-239
    • De Boer, A.L.1    Neerken, S.2    De Wijn, R.3    Permentier, H.P.4    Gast, P.5    Vijgenboom, E.6    Hoff, A.J.7
  • 36
    • 0025114451 scopus 로고
    • Effect of specific mutations of tyrosine-(M)210 on the primary photosynthetic electron-transfer process in Rhodobacter sphaeroides
    • Nagarajan, V., Parson, W. W., Gaul, D., and Schenck, C. (1990) Effect of specific mutations of tyrosine-(M)210 on the primary photosynthetic electron-transfer process in Rhodobacter sphaeroides, Proc. Natl. Acad. Sci. U.S.A. 87, 7888-7892.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 7888-7892
    • Nagarajan, V.1    Parson, W.W.2    Gaul, D.3    Schenck, C.4
  • 37
    • 0025196834 scopus 로고
    • Role of tyrosine M210 in the initial charge separation of reaction centers of Rhodobacter sphaeroides
    • Finkele, U., Lauterwasser, C., Zinth, W., Gray, K. A., and Oesterhelt, D. (1990) Role of tyrosine M210 in the initial charge separation of reaction centers of Rhodobacter sphaeroides, Biochemistry 29, 8517-8521.
    • (1990) Biochemistry , vol.29 , pp. 8517-8521
    • Finkele, U.1    Lauterwasser, C.2    Zinth, W.3    Gray, K.A.4    Oesterhelt, D.5
  • 40
    • 0026769095 scopus 로고
    • Photochemical trapping of a bacteriopheophytin anion in site-specific reaction-center mutants from the photosynthetic bacterium Rhodobacter sphaeroides
    • Gray, K. A., Wachtveitl, J., and Oesterhelt, D. (1992) Photochemical trapping of a bacteriopheophytin anion in site-specific reaction-center mutants from the photosynthetic bacterium Rhodobacter sphaeroides, Eur. J. Biochem. 207, 723-731.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 723-731
    • Gray, K.A.1    Wachtveitl, J.2    Oesterhelt, D.3
  • 42
    • 0027519330 scopus 로고
    • Kinetics and free energy of electron-transfer reactions in Rhodobacter sphaeroides reaction centers
    • Nagarajan, V., Parson, W. W., Davis, D., and Schenck, C. C. (1993) Kinetics and free energy of electron-transfer reactions in Rhodobacter sphaeroides reaction centers, Biochemistry 32, 12324-12336.
    • (1993) Biochemistry , vol.32 , pp. 12324-12336
    • Nagarajan, V.1    Parson, W.W.2    Davis, D.3    Schenck, C.C.4
  • 44
    • 0030260337 scopus 로고    scopus 로고
    • Orientation of the OH dipole of tyrosine (M)210 and its effect on electrostatic energies in photosynthetic bacterial reaction centers
    • Alden, R. G., Parson, W. W., Chu, Z. T., and Warshel, A. (1996) Orientation of the OH dipole of tyrosine (M)210 and its effect on electrostatic energies in photosynthetic bacterial reaction centers, J. Phys. Chem. 100, 16761-16770.
    • (1996) J. Phys. Chem. , vol.100 , pp. 16761-16770
    • Alden, R.G.1    Parson, W.W.2    Chu, Z.T.3    Warshel, A.4
  • 46
    • 0030859058 scopus 로고    scopus 로고
    • Antenna excited-state decay kinetics establish primary electron transfer in reaction centers as heterogeneous
    • Laible, P. D., Greenfield, S. R., Wasielewski, M. R., Hanson, D. K., and Pearlstein, R. M. (1997) Antenna excited-state decay kinetics establish primary electron transfer in reaction centers as heterogeneous, Biochemistry 36, 8677-8685.
    • (1997) Biochemistry , vol.36 , pp. 8677-8685
    • Laible, P.D.1    Greenfield, S.R.2    Wasielewski, M.R.3    Hanson, D.K.4    Pearlstein, R.M.5
  • 47
    • 0001136184 scopus 로고    scopus 로고
    • Protein-chromophore interactions: Spectral shifts report the consequences of mutations in the bacterial photosynthetic reaction center
    • DiMagno, T. J., Laible, P. D., Reddy, N. R., Small, G. J., Norris, J. R., Schiffer, M., and Hanson, D. K. (1998) Protein-chromophore interactions: spectral shifts report the consequences of mutations in the bacterial photosynthetic reaction center, Spectrochim. Acta A54, 1247-1267.
    • (1998) Spectrochim. Acta , vol.A54 , pp. 1247-1267
    • DiMagno, T.J.1    Laible, P.D.2    Reddy, N.R.3    Small, G.J.4    Norris, J.R.5    Schiffer, M.6    Hanson, D.K.7
  • 48
    • 0000191516 scopus 로고    scopus 로고
    • B-A and B-B absorbance perturbations induced by coherent nuclear motions in reaction centers from Rhodobacter sphaeroides upon 30-fs excitation of the primary donor
    • Streltsov, A. M., Vulto, S. I. E., Shkuropatov, A. Y., Hoff, A. J., Aartsma, T. J., and Shuvalov, V. A. (1998) B-A and B-B absorbance perturbations induced by coherent nuclear motions in reaction centers from Rhodobacter sphaeroides upon 30-fs excitation of the primary donor, J. Phys. Chem. 102, 7293-7298.
    • (1998) J. Phys. Chem. , vol.102 , pp. 7293-7298
    • Streltsov, A.M.1    Vulto, S.I.E.2    Shkuropatov, A.Y.3    Hoff, A.J.4    Aartsma, T.J.5    Shuvalov, V.A.6
  • 49
    • 0001682402 scopus 로고    scopus 로고
    • Probing excited-state electron transfer by resonance Stark spectroscopy. 1. Experimental results for photosynthetic reaction centers
    • Zhou, H., and Boxer, S. G. (1998) Probing excited-state electron transfer by resonance Stark spectroscopy. 1. Experimental results for photosynthetic reaction centers, J. Phys. Chem. 102, 9139-9147.
    • (1998) J. Phys. Chem. , vol.102 , pp. 9139-9147
    • Zhou, H.1    Boxer, S.G.2
  • 50
    • 0023147801 scopus 로고
    • Isolation and spectroscopic properties of photochemical reaction centers from Rhodobacter capsulatus
    • Prince, R. C., and Youvan, D. C. (1987) Isolation and spectroscopic properties of photochemical reaction centers from Rhodobacter capsulatus, Biochim. Biophys. Acta 890, 286-291.
    • (1987) Biochim. Biophys. Acta , vol.890 , pp. 286-291
    • Prince, R.C.1    Youvan, D.C.2
  • 51
    • 0028322383 scopus 로고
    • Comparative study of reaction centers from purple photosynthetic bacteria: Isolation and spectroscopy
    • Wang, S., Lin, S., Woodbury, N. W., and Allen, J. P. (1994) Comparative study of reaction centers from purple photosynthetic bacteria: isolation and spectroscopy, Photosyn. Res. 42, 203-215.
    • (1994) Photosyn. Res. , vol.42 , pp. 203-215
    • Wang, S.1    Lin, S.2    Woodbury, N.W.3    Allen, J.P.4
  • 52
    • 0000178540 scopus 로고
    • Primary acceptor in bacterial photosynthesis: Obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas spheroides
    • Okamura, M. Y., Isaacson, R. A., and Feher, G. (1975) Primary acceptor in bacterial photosynthesis: obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas spheroides, Proc. Natl. Acad. Sci. U.S.A. 72, 3492-3495.
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 3492-3495
    • Okamura, M.Y.1    Isaacson, R.A.2    Feher, G.3
  • 54
    • 84970058986 scopus 로고
    • A genetic system for rapidly assessing herbicides that compete for the quinone binding site of photosynthetic reaction centers
    • Bylina, E. J., Jovine, R. V. M., and Youvan, D. C. (1989) A genetic system for rapidly assessing herbicides that compete for the quinone binding site of photosynthetic reaction centers, Bio/Technology 7, 69-74.
    • (1989) Bio/Technology , vol.7 , pp. 69-74
    • Bylina, E.J.1    Jovine, R.V.M.2    Youvan, D.C.3
  • 55
    • 85005726073 scopus 로고
    • Directed mutations affecting the putative bacteriochlorophyll-binding sites in the light-harvesting I antenna of Rhodobacter capsulatus
    • Bylina, E. J., Robles, S. J., and Youvan, D. C. (1988) Directed mutations affecting the putative bacteriochlorophyll-binding sites in the light-harvesting I antenna of Rhodobacter capsulatus, Isr. J. Chem. 28, 73-78.
    • (1988) Isr. J. Chem. , vol.28 , pp. 73-78
    • Bylina, E.J.1    Robles, S.J.2    Youvan, D.C.3
  • 56
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria
    • Simon, R., Priefer, U., and Puhler, A. (1983) A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria, Bio/Technology 1, 37-45.
    • (1983) Bio/Technology , vol.1 , pp. 37-45
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 57
    • 0022344842 scopus 로고
    • Chromosomal deletion and plasmid complementation of the photosynthetic reaction center and light-harvesting genes from Rhodopseudomonas capsulata
    • Youvan, D. C., Ismail, S., and Bylina, E. J. (1985) Chromosomal deletion and plasmid complementation of the photosynthetic reaction center and light-harvesting genes from Rhodopseudomonas capsulata, Gene 33, 19-30.
    • (1985) Gene , vol.33 , pp. 19-30
    • Youvan, D.C.1    Ismail, S.2    Bylina, E.J.3
  • 58
    • 0016720598 scopus 로고
    • Characterization of Rhodopseudomonas capsulata
    • Weaver, P. F., Wall, J. D., and Gest, H. (1975) Characterization of Rhodopseudomonas capsulata, Arch. Microbiol. 105, 207-216.
    • (1975) Arch. Microbiol. , vol.105 , pp. 207-216
    • Weaver, P.F.1    Wall, J.D.2    Gest, H.3
  • 60
    • 0002652674 scopus 로고
    • On the role of tryptophan as a superexchange mediator for quinone reduction in photosynthetic reaction centers
    • Plato, M., Michel-Beyerle, M. E., Bixon, M., and Jortner, J. (1989) On the role of tryptophan as a superexchange mediator for quinone reduction in photosynthetic reaction centers, FEBS Lett. 249, 70-74.
    • (1989) FEBS Lett. , vol.249 , pp. 70-74
    • Plato, M.1    Michel-Beyerle, M.E.2    Bixon, M.3    Jortner, J.4
  • 62
    • 0002263704 scopus 로고
    • Site-directed mutagenesis of threonine M222 and tryptophan M252 in the photosynthetic reaction center of Rhodobacter sphaeroides
    • Michel-Beyerle, M. E., Ed., Springer-Verlag, New York
    • Stilz, H. Y., Finkele, U., Holzapfel, W., Lauterwasser, C., Zinth, W., and Oesterhelt, D. (1990) Site-directed mutagenesis of threonine M222 and tryptophan M252 in the photosynthetic reaction center of Rhodobacter sphaeroides, In Structure and Function of Bacterial Photosynthetic Reaction Centers (Michel-Beyerle, M. E., Ed.) pp 265-271, Springer-Verlag, New York.
    • (1990) Structure and Function of Bacterial Photosynthetic Reaction Centers , pp. 265-271
    • Stilz, H.Y.1    Finkele, U.2    Holzapfel, W.3    Lauterwasser, C.4    Zinth, W.5    Oesterhelt, D.6
  • 63
    • 0028359506 scopus 로고
    • Influence of M subunit Thr222 and Trp252 on quinone binding and electron transfer in Rhodobacter sphaeroides reaction centres
    • Stilz, H. U., Finkele, U., Holzapfel, W., Lauterwasser, C., Zinth, W., and Oesterhelt, D. (1994) Influence of M subunit Thr222 and Trp252 on quinone binding and electron transfer in Rhodobacter sphaeroides reaction centres, Eur. J. Biochem. 223, 233-242.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 233-242
    • Stilz, H.U.1    Finkele, U.2    Holzapfel, W.3    Lauterwasser, C.4    Zinth, W.5    Oesterhelt, D.6
  • 64
    • 0038068675 scopus 로고
    • Reconstitution of photochemical activity in Rhodobacter capsulatus reaction centers containing mutation at tryptophan M-250 in the primary quinone binding site
    • Baltscheffsky, M., Ed., Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Coleman, W. J., Bylina, E. J., and Youvan, D. C. (1990) Reconstitution of photochemical activity in Rhodobacter capsulatus reaction centers containing mutation at tryptophan M-250 in the primary quinone binding site, In Current Research in Photosynthesis (Baltscheffsky, M., Ed.) pp 149-152, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1990) Current Research in Photosynthesis , pp. 149-152
    • Coleman, W.J.1    Bylina, E.J.2    Youvan, D.C.3
  • 65
    • 0028046488 scopus 로고
    • Comparative study of reaction centers from photosynthetic purple bacteria: Electron paramagnetic resonance and electron nuclear double resonance spectroscopy
    • Rautter, J., Lendzian, F., Lubitz, W., Wang, S., and Allen, J. P. (1994) Comparative study of reaction centers from photosynthetic purple bacteria: Electron paramagnetic resonance and electron nuclear double resonance spectroscopy, Biochemistry 33, 12077-12084.
    • (1994) Biochemistry , vol.33 , pp. 12077-12084
    • Rautter, J.1    Lendzian, F.2    Lubitz, W.3    Wang, S.4    Allen, J.P.5
  • 69
    • 0023048040 scopus 로고
    • Radical-pair energetics and decay mechanisms in reaction centers containing anthraquinones, naphthoquinones, or benzoquinones in place of ubiquinone
    • Woodbury, N. W., Parson, W. W., Gunner, M., Prince, R. A., and Dutton, P. L. (1986) Radical-pair energetics and decay mechanisms in reaction centers containing anthraquinones, naphthoquinones, or benzoquinones in place of ubiquinone, Biochim. Biophys. Acta 851, 16-22.
    • (1986) Biochim. Biophys. Acta , vol.851 , pp. 16-22
    • Woodbury, N.W.1    Parson, W.W.2    Gunner, M.3    Prince, R.A.4    Dutton, P.L.5
  • 73
    • 0031858373 scopus 로고    scopus 로고
    • Free energy dependence of the direct charge recombination from primary and secondary quinones in reaction centers from Rhodobacter sphaeroides
    • Allen, J. P., Williams, J. C., Graige, M. S., Paddock, M. L., Labahn, A., Feher, G., and Okamura, M. Y. (1998) Free energy dependence of the direct charge recombination from primary and secondary quinones in reaction centers from Rhodobacter sphaeroides, Photosyn. Res. 55, 227-233.
    • (1998) Photosyn. Res. , vol.55 , pp. 227-233
    • Allen, J.P.1    Williams, J.C.2    Graige, M.S.3    Paddock, M.L.4    Labahn, A.5    Feher, G.6    Okamura, M.Y.7
  • 74
    • 0025977598 scopus 로고
    • Heterogeneity of kinetics and electron-transfer equilibria in the bacteriopheophytin and quinone electron acceptors of reaction centers from Rhodopseudomonas viridis
    • Gao, J.-L., Shopes, R. J., and Wraight, C. A. (1991) Heterogeneity of kinetics and electron-transfer equilibria in the bacteriopheophytin and quinone electron acceptors of reaction centers from Rhodopseudomonas viridis, Biochim. Biophys. Acta 1056, 259-272.
    • (1991) Biochim. Biophys. Acta , vol.1056 , pp. 259-272
    • Gao, J.-L.1    Shopes, R.J.2    Wraight, C.A.3
  • 75
    • 0013244298 scopus 로고
    • Charges recombination kinetics in bacterial photosynthetic reaction centers: Conformational states in equilibrium preexist in the dark
    • Breton, J., and Vermeglio, A., Eds., Plenum Press, New York
    • Schoepp, B., Parot, P., Lavorel, J., and Vermeglio, A. (1992) Charges recombination kinetics in bacterial photosynthetic reaction centers: Conformational states in equilibrium preexist in the dark, In The Photosynthetic Bacterial Reaction Center II: Structure, Spectroscopy, and Dynamics (Breton, J., and Vermeglio, A., Eds.) pp 331-339, Plenum Press, New York.
    • (1992) The Photosynthetic Bacterial Reaction Center II: Structure, Spectroscopy, and Dynamics , pp. 331-339
    • Schoepp, B.1    Parot, P.2    Lavorel, J.3    Vermeglio, A.4
  • 76
    • 0028851382 scopus 로고
    • Heterogeneity of the quinone electron acceptor system in bacterial reaction centers
    • Baciou, L., and Sebban, P. (1995) Heterogeneity of the quinone electron acceptor system in bacterial reaction centers, Photochem. Photobiol. 62, 271-278.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 271-278
    • Baciou, L.1    Sebban, P.2
  • 77
    • 0013303317 scopus 로고
    • Protein relaxation following quinone reduction in Rhodobacter capsulatus: Detection of likely protonation-linked optical absorbance changes of the chromatophores
    • Breton, J., and Vermeglio, A., Eds., Plenum, New York
    • Tiede, D. M., and Hanson, D. K. (1992) Protein relaxation following quinone reduction in Rhodobacter capsulatus: Detection of likely protonation-linked optical absorbance changes of the chromatophores. In The Photosynthetic Bacterial Reaction Center II (Breton, J., and Vermeglio, A., Eds.) pp 341-350, Plenum, New York.
    • (1992) The Photosynthetic Bacterial Reaction Center II , pp. 341-350
    • Tiede, D.M.1    Hanson, D.K.2
  • 78
    • 0031830449 scopus 로고    scopus 로고
    • Resolution of electron and proton-transfer events in the electrochromism associated with quinone reduction in bacterial reaction centers
    • Tiede, D. M., Utschig, L., Hanson, D. K., and Gallo, D. M. (1998) Resolution of electron and proton-transfer events in the electrochromism associated with quinone reduction in bacterial reaction centers, Photosyn. Res. 55, 267-273.
    • (1998) Photosyn. Res. , vol.55 , pp. 267-273
    • Tiede, D.M.1    Utschig, L.2    Hanson, D.K.3    Gallo, D.M.4
  • 79
    • 0038479088 scopus 로고    scopus 로고
    • Conformation-activated protonation in reaction centers of the photosynthetic bacterium Rhodobacter sphaeroides
    • Kálmán. L., and Maróti, P. (1997) Conformation-activated protonation in reaction centers of the photosynthetic bacterium Rhodobacter sphaeroides, Biochemistry 36, 15269-15276.
    • (1997) Biochemistry , vol.36 , pp. 15269-15276
    • Kálmán, L.1    Maróti, P.2
  • 80
    • 0033264483 scopus 로고    scopus 로고
    • Proton binding is part of protein relaxation of flash-excited reaction center from photosynthetic bacteria Rhodobacter sphaeroides
    • Turzo, K., Laczko, G., and Maróti, P. (1999) Proton binding is part of protein relaxation of flash-excited reaction center from photosynthetic bacteria Rhodobacter sphaeroides, Isr. J. Chem. 39, 447-455.
    • (1999) Isr. J. Chem. , vol.39 , pp. 447-455
    • Turzo, K.1    Laczko, G.2    Maróti, P.3
  • 81
    • 0033430414 scopus 로고    scopus 로고
    • Proton uptake by bacterial reaction centers: The protein complex responds in a manner similar to the reduction of either quinone acceptor
    • Miksovska. J., Schiffer, M., Hanson, D. K., and Sebban, P. (1999) Proton uptake by bacterial reaction centers: The protein complex responds in a manner similar to the reduction of either quinone acceptor, Proc. Natl. Acad. Sci. U.S.A. 96, 14348-14353.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 14348-14353
    • Miksovska, J.1    Schiffer, M.2    Hanson, D.K.3    Sebban, P.4
  • 82
    • 0035918351 scopus 로고    scopus 로고
    • 2+ site in photosynthetic bacterial reaction centers from Rhodobacter sphaeroides, Rhodobacter capsulatus, and Rhodopseudomonas viridis
    • 2+ site in photosynthetic bacterial reaction centers from Rhodobacter sphaeroides, Rhodobacter capsulatus, and Rhodopseudomonas viridis, Biochemistry 40, 6132-6141.
    • (2001) Biochemistry , vol.40 , pp. 6132-6141
    • Utschig, L.M.1    Poluektov, O.2    Schlesselman, S.L.3    Thurnauer, M.C.4    Tiede, D.M.5
  • 83
    • 0037176849 scopus 로고    scopus 로고
    • B electron-transfer reaction in bacterial photosynthetic reaction centers: pH dependence of the conformational gating step
    • B electron-transfer reaction in bacterial photosynthetic reaction centers: pH dependence of the conformational gating step, Biochemistry 41, 2694-2701.
    • (2002) Biochemistry , vol.41 , pp. 2694-2701
    • Xu, Q.1    Gunner, M.R.2
  • 84
    • 0037031293 scopus 로고    scopus 로고
    • B electron transfer in bacterial photosynthetic reaction centers: Effect of substrate position and tail length on the conformational gating step
    • B electron transfer in bacterial photosynthetic reaction centers: effect of substrate position and tail length on the conformational gating step, Biochemistry 41, 10021-10025.
    • (2002) Biochemistry , vol.41 , pp. 10021-10025
    • Xu, Q.1    Baciou, L.2    Sebban, P.3    Gunner, M.R.4
  • 85
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron - Proton transfer
    • Stowell, M. H. B., McPhillips, T. M., Rees, D. C., Soltis, S. M., Abresch, E., and Feher, G. (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.B.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 87
    • 0037076542 scopus 로고    scopus 로고
    • The structure of a mutant photosynthetic reaction center shows unexpected changes in main chain orientations and quinone position
    • Pokkuluri, P. R., Laible, P. D., Deng, Y. L., Wong, T. N., Hanson, D. K., and Schiffer, M. (2002) The structure of a mutant photosynthetic reaction center shows unexpected changes in main chain orientations and quinone position, Biochemistry 41, 5998-6007.
    • (2002) Biochemistry , vol.41 , pp. 5998-6007
    • Pokkuluri, P.R.1    Laible, P.D.2    Deng, Y.L.3    Wong, T.N.4    Hanson, D.K.5    Schiffer, M.6
  • 88
    • 0036795645 scopus 로고    scopus 로고
    • Charge separation induces conformational changes in the photosynthetic reaction centre of purple bacteria
    • Fritzsch, G., Koepke, J., Diem, R., Kuglstatter, A., and Baciou, L. (2002) Charge separation induces conformational changes in the photosynthetic reaction centre of purple bacteria, Acta Crystallogr. D 58, 1660-1663.
    • (2002) Acta Crystallogr. D , vol.58 , pp. 1660-1663
    • Fritzsch, G.1    Koepke, J.2    Diem, R.3    Kuglstatter, A.4    Baciou, L.5
  • 89
    • 0021674417 scopus 로고
    • Electrontransfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: Evidence for light-induced structural changes
    • Kleinfeld, D., Okamura, M. Y., and Feher, G. (1984) Electrontransfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: Evidence for light-induced structural changes, Biochemistry 23, 5780-5786.
    • (1984) Biochemistry , vol.23 , pp. 5780-5786
    • Kleinfeld, D.1    Okamura, M.Y.2    Feher, G.3
  • 90
    • 0032578541 scopus 로고    scopus 로고
    • - in bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay
    • - in bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay, Proc. Natl. Acad. Sci. U.S.A. 95, 11679-11684.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 11679-11684
    • Graige, M.S.1    Feher, G.2    Okamura, M.Y.3
  • 92
    • 0035836485 scopus 로고    scopus 로고
    • X-ray structure analyses of photosynthetic reaction center variants from Rhodobacter sphaeroides: Structural changes induced by point mutations at position L209 modulate electron and proton transfer
    • Kuglstatter, A., Ermler, U., Michel, H., Baciou, L., and Fritzsch, G. (2001) X-ray structure analyses of photosynthetic reaction center variants from Rhodobacter sphaeroides: Structural changes induced by point mutations at position L209 modulate electron and proton transfer, Biochemistry 40, 4253-4260.
    • (2001) Biochemistry , vol.40 , pp. 4253-4260
    • Kuglstatter, A.1    Ermler, U.2    Michel, H.3    Baciou, L.4    Fritzsch, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.