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Volumn 46, Issue 51, 2007, Pages 14782-14794

Low-temperature pulsed EPR study at 34 GHz of the triplet states of the primary electron donor P865 and the carotenoid in native and mutant bacterial reaction centers of Rhodobacter sphaeroides

Author keywords

[No Author keywords available]

Indexed keywords

CAROTENOID PIGMENTS; ELECTRON DONOR; RHODOBACTER SPHAEROIDES;

EID: 37349051388     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701593r     Document Type: Article
Times cited : (17)

References (68)
  • 2
    • 77951507246 scopus 로고
    • ESR study of the photoexcited triplet state in photosynthetic bacteria
    • Thurnauer, M. C. (1979) ESR study of the photoexcited triplet state in photosynthetic bacteria, Rev. Chem. Int. 100, 197-231.
    • (1979) Rev. Chem. Int , vol.100 , pp. 197-231
    • Thurnauer, M.C.1
  • 3
    • 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
  • 4
    • 0002163157 scopus 로고
    • Chlorophyll triplets and radical pairs
    • Scheer, H, Ed, pp, CRC Press, Boca Raton, FL
    • Angerhofer, A. (1991) Chlorophyll triplets and radical pairs, in Chlorophylls (Scheer, H., Ed.) pp 945-991, CRC Press, Boca Raton, FL.
    • (1991) Chlorophylls , pp. 945-991
    • Angerhofer, A.1
  • 5
    • 0000058886 scopus 로고
    • Structure and function of bacterial photosynthetic reaction centers
    • Feher, G., Allen, J. P., Okamura, M. Y., and Rees, D. C. (1989) Structure and function of bacterial photosynthetic reaction centers, Nature 339, 111-116.
    • (1989) Nature , vol.339 , pp. 111-116
    • Feher, G.1    Allen, J.P.2    Okamura, M.Y.3    Rees, D.C.4
  • 6
    • 4043177322 scopus 로고
    • Photoexcited triplet-state and photosynthesis
    • Levanon, H., and Norris, J. R. (1978) Photoexcited triplet-state and photosynthesis, Chem. Rev. 78, 185-198.
    • (1978) Chem. Rev , vol.78 , pp. 185-198
    • Levanon, H.1    Norris, J.R.2
  • 7
    • 0026069087 scopus 로고
    • The chlorophyll triplet-state as a probe of structure and function in photosynthesis
    • Budil, D. E., and Thurnauer, M. C. (1991) The chlorophyll triplet-state as a probe of structure and function in photosynthesis, Biochim. Biophys. Acta 1057, 1-41.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 1-41
    • Budil, D.E.1    Thurnauer, M.C.2
  • 8
    • 0021755973 scopus 로고
    • X-ray structure-analysis of a membrane-protein complex - electron-density map at 3A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomo nas viridis
    • Deisenhofer, J., Epp, O., Miki, K., Huber, R., and Michel, H. (1984) X-ray structure-analysis of a membrane-protein complex - electron-density map at 3A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomo nas viridis, J. Mol. Biol. 180, 385-398.
    • (1984) J. Mol. Biol , vol.180 , pp. 385-398
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 9
    • 0020475570 scopus 로고
    • 3-Dimensional crystals of a membrane-protein complex - the photosynthetic reaction center from Rhodopseudomonas viridis
    • Michel, H. (1982) 3-Dimensional crystals of a membrane-protein complex - the photosynthetic reaction center from Rhodopseudomonas viridis, J. Mol. Biol. 158, 567-572.
    • (1982) J. Mol. Biol , vol.158 , pp. 567-572
    • Michel, H.1
  • 10
    • 0023408258 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26 - the protein subunits
    • 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 protein subunits, Proc. Natl. Acad. Sci. U.S.A. 84, 6162-6166.
    • (1987) Proc. Natl. Acad. Sci. U.S.A , vol.84 , pp. 6162-6166
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 11
    • 0024110321 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26 - protein cofactor (quinones and Fe-2+) interactions
    • Allen, J. P., Feher, G., Yeates, T. O., Komiya, H., and Rees, D. C. (1988) Structure of the reaction center from Rhodobacter sphaeroides R-26 - protein cofactor (quinones and Fe-2+) interactions, Proc. Natl. Acad. Sci. U.S.A. 85, 8487-8491.
    • (1988) Proc. Natl. Acad. Sci. U.S.A , vol.85 , pp. 8487-8491
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 12
    • 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., Komiya, H., Chirino, A., Rees, D. C., Allen, J. P., and Feher, G. (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. U.S.A. 85, 7993-7997.
    • (1988) Proc. Natl. Acad. Sci. U.S.A , vol.85 , pp. 7993-7997
    • Yeates, T.O.1    Komiya, H.2    Chirino, A.3    Rees, D.C.4    Allen, J.P.5    Feher, G.6
  • 13
    • 0031646685 scopus 로고    scopus 로고
    • Energetics and mechanism of primary charge separation in bacterial photosynthesis. A comparative study on reaction centers of Rhodobacter sphaeroides and Chloroflexus aurantiacus
    • Volk, M., Aumeier, G., Langenbacher, T., Feick, R., Ogrodnik, A., and Michel-Beyerle, M. E. (1998) Energetics and mechanism of primary charge separation in bacterial photosynthesis. A comparative study on reaction centers of Rhodobacter sphaeroides and Chloroflexus aurantiacus, J. Phys. Chem. B 102, 735-751.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 735-751
    • Volk, M.1    Aumeier, G.2    Langenbacher, T.3    Feick, R.4    Ogrodnik, A.5    Michel-Beyerle, M.E.6
  • 14
    • 0000555043 scopus 로고    scopus 로고
    • Magnetophotoselection study of the lowest excited triplet state of the primary donor in photosynthetic bacteria
    • Borovykh, I. V., Proskuryakov, I. I., Klenina, I. B., Gast, P., and Hoff, A. J. (2000) Magnetophotoselection study of the lowest excited triplet state of the primary donor in photosynthetic bacteria, J. Phys. Chem. B 104, 4222-4228.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 4222-4228
    • Borovykh, I.V.1    Proskuryakov, I.I.2    Klenina, I.B.3    Gast, P.4    Hoff, A.J.5
  • 15
    • 18244409359 scopus 로고    scopus 로고
    • Quinone (Q(B)) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: Quantum efficiency and X-ray structure
    • Paddock, M. L., Chang, C., Xu, Q., Abresch, E. C., Axelrod, H. L., Feher, G., and Okamura, M. Y. (2005) Quinone (Q(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    Feher, G.6    Okamura, M.Y.7
  • 16
    • 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, Photosynth. Res. 71, 221-239.
    • (2002) Photosynth. 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
  • 17
    • 34248230651 scopus 로고    scopus 로고
    • Protein dynamics control the kinetics of initial electron transfer in photosynthesis
    • Wang, H. Y., Lin, S., Allen, J. P., Williams, J. C., Blankert, S., Laser, C., and Woodbury, N. W. (2007) Protein dynamics control the kinetics of initial electron transfer in photosynthesis, Science 316, 747-750.
    • (2007) Science , vol.316 , pp. 747-750
    • Wang, H.Y.1    Lin, S.2    Allen, J.P.3    Williams, J.C.4    Blankert, S.5    Laser, C.6    Woodbury, N.W.7
  • 18
    • 0000093210 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., Laporte, L., Schenck, C. C., and Holten, D. (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
  • 19
    • 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., Laporte, L., Schenck, C. C., and Holten, D. (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. 99, 8910-8917.
    • (1995) J. Phys. Chem , vol.99 , pp. 8910-8917
    • Kirmaier, C.1    Laporte, L.2    Schenck, C.C.3    Holten, D.4
  • 20
    • 0029647453 scopus 로고
    • Control of electron-transfer between the L-side and M-side of photosynthetic reaction centers
    • Heller, B. A., Holten, D., and Kirmaier, C. (1995) Control of electron-transfer between the L-side and M-side 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
  • 21
    • 0344925572 scopus 로고    scopus 로고
    • High yield of long-lived B-side charge separation at room temperature in mutant bacterial reaction centers
    • Haffa, A. L. M., Lin, S., Williams, J. C., Taguchi, A. K. W., Allen, J. P., and Woodbury, N. W. (2003) High yield of long-lived B-side charge separation at room temperature in mutant bacterial reaction centers, J. Phys. Chem. B 107, 12503-12510.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 12503-12510
    • Haffa, A.L.M.1    Lin, S.2    Williams, J.C.3    Taguchi, A.K.W.4    Allen, J.P.5    Woodbury, N.W.6
  • 22
    • 0035923418 scopus 로고    scopus 로고
    • Blue light drives B-side electron transfer in bacterial photosynthetic reaction centers
    • Lin, S., Katilius, E., Haffa, A. L. M., Taguchi, A. K. W., 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.M.3    Taguchi, A.K.W.4    Woodbury, N.W.5
  • 23
    • 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
  • 24
    • 33645453302 scopus 로고    scopus 로고
    • High yield of M-side electron transfer in mutants of Rhodobacter capsulatus reaction centers lacking the L-side bacteriopheophytin
    • Chuang, J. I., Boxer, S. G., Holten, D., and Kirmaier, C. (2006) High yield of M-side electron transfer in mutants of Rhodobacter capsulatus reaction centers lacking the L-side bacteriopheophytin, Biochemistry 45, 3845-3851.
    • (2006) Biochemistry , vol.45 , pp. 3845-3851
    • Chuang, J.I.1    Boxer, S.G.2    Holten, D.3    Kirmaier, C.4
  • 25
    • 0035999847 scopus 로고    scopus 로고
    • Radicals, radical pairs and triplet states in photosynthesis
    • Lubitz, W., Lendzian, F., and Bittl, R. (2002) Radicals, radical pairs and triplet states in photosynthesis, Acc. Chem. Res. 35, 313-320.
    • (2002) Acc. Chem. Res , vol.35 , pp. 313-320
    • Lubitz, W.1    Lendzian, F.2    Bittl, R.3
  • 26
    • 0032897689 scopus 로고    scopus 로고
    • Mutations that modify or exclude binding of the QA ubiquinone and carotenoid in the reaction center from Rhodobacter sphaeroides
    • Ridge, J. P., van Brederode, M. E., Goodwin, M. G., van Grondelle, R., and Jones, M. R. (1999) Mutations that modify or exclude binding of the QA ubiquinone and carotenoid in the reaction center from Rhodobacter sphaeroides, Photosynth. Res. 59, 9-26.
    • (1999) Photosynth. Res , vol.59 , pp. 9-26
    • Ridge, J.P.1    van Brederode, M.E.2    Goodwin, M.G.3    van Grondelle, R.4    Jones, M.R.5
  • 27
    • 0001153887 scopus 로고
    • Transient electron-spin resonance spectroscopy of the carotenoid triplet-state in Rhodopseudomonas sphaeroides wild-type
    • McGann, W. J., and Frank, H. A. (1985) Transient electron-spin resonance spectroscopy of the carotenoid triplet-state in Rhodopseudomonas sphaeroides wild-type, Chem. Phys. Lett. 121, 253-261.
    • (1985) Chem. Phys. Lett , vol.121 , pp. 253-261
    • McGann, W.J.1    Frank, H.A.2
  • 28
    • 0001160928 scopus 로고
    • Triplet electron- paramagnetic-res spectra of the primary electron-donor in bacterial photosynthesis at temperatures between 15-K and 296-K
    • Hoff, A. J., and Proskuryakov, I. I. (1985) Triplet electron- paramagnetic-res spectra of the primary electron-donor in bacterial photosynthesis at temperatures between 15-K and 296-K, Chem. Phys. Lett. 115, 303-310.
    • (1985) Chem. Phys. Lett , vol.115 , pp. 303-310
    • Hoff, A.J.1    Proskuryakov, I.I.2
  • 29
    • 0001478685 scopus 로고
    • Electron-paramagnetic resonance detection of carotenoid triplet-states
    • Frank, H. A., Bolt, J. D., Costa, S. M. D. B., and Sauer, K. (1980) Electron-paramagnetic resonance detection of carotenoid triplet-states, J. Am. Chem. Soc. 102, 4893-4898.
    • (1980) J. Am. Chem. Soc , vol.102 , pp. 4893-4898
    • Frank, H.A.1    Bolt, J.D.2    Costa, S.M.D.B.3    Sauer, K.4
  • 30
    • 0000259541 scopus 로고
    • Carotenoid triplet-state formation in Rhodobacter sphaeroides R-26 reaction centers exchanged with modified bacteriochlorophyll pigments and reconstituted with spheroidene
    • Frank, H. A., Chynwat, V., Hartwich, G., Meyer, M., Katheder, I., and Scheer, H. (1993) Carotenoid triplet-state formation in Rhodobacter sphaeroides R-26 reaction centers exchanged with modified bacteriochlorophyll pigments and reconstituted with spheroidene, Photosynth. Res. 37, 193-203.
    • (1993) Photosynth. Res , vol.37 , pp. 193-203
    • Frank, H.A.1    Chynwat, V.2    Hartwich, G.3    Meyer, M.4    Katheder, I.5    Scheer, H.6
  • 31
    • 0002565845 scopus 로고
    • Analysis of polarized EPR spectra
    • Hoff, A, Ed, pp, Elsevier, Amsterdam
    • Hore, P. J. (1990) Analysis of polarized EPR spectra, in Advanced EPR in Biology and Biochemistry (Hoff, A., Ed.) pp 405-440, Elsevier, Amsterdam.
    • (1990) Advanced EPR in Biology and Biochemistry , pp. 405-440
    • Hore, P.J.1
  • 32
    • 0003086416 scopus 로고
    • Chemical composition and properties of reaction centers
    • Clayton, R. and Sistrom, W, Eds, pp, Plenum Press, New York
    • Feher, G., and Okamura, M. (1978) Chemical composition and properties of reaction centers, in The Photosynthetic Bacteria (Clayton, R. and Sistrom, W., Eds.) pp 349-386, Plenum Press, New York.
    • (1978) The Photosynthetic Bacteria , pp. 349-386
    • Feher, G.1    Okamura, M.2
  • 34
    • 0031855897 scopus 로고    scopus 로고
    • Pulsed ENDOR of the photoexcited triplet states of bacteriochlorophyll a and of the primary donor P-865 in reaction centers of Rhodobacter sphaeroides R-26
    • Lendzian, F., Bittl, R., and Lubitz, W. (1998) Pulsed ENDOR of the photoexcited triplet states of bacteriochlorophyll a and of the primary donor P-865 in reaction centers of Rhodobacter sphaeroides R-26, Photosynth. Res. 55, 189-197.
    • (1998) Photosynth. Res , vol.55 , pp. 189-197
    • Lendzian, F.1    Bittl, R.2    Lubitz, W.3
  • 35
    • 0038860930 scopus 로고
    • Magnetic resonance and molecular orbital studies of the primary donor states in bacterial reaction centers
    • Jortner, J, and Pullman, B, Eds, pp, Kluwer Academic Publishers, Dordrecht
    • Plato, M., Möbius, K., Lubitz, W., Allen, J. P., and Feher, G. (1990) Magnetic resonance and molecular orbital studies of the primary donor states in bacterial reaction centers, in Perspectives in Photosynthesis (Jortner, J., and Pullman, B., Eds.) pp 423-434, Kluwer Academic Publishers, Dordrecht.
    • (1990) Perspectives in Photosynthesis , pp. 423-434
    • Plato, M.1    Möbius, K.2    Lubitz, W.3    Allen, J.P.4    Feher, G.5
  • 36
    • 0040639194 scopus 로고
    • ENDOR and TRIPLE resonance investigation of the primary donor cation radical P865 in single crystals of Rhodobacter sphaeroides R-26 reaction centers
    • Michel-Beyerle, M. E, Ed, pp, Springer-Verlag, Berlin
    • Lendzian, F., Endeward, B., Plato, M., Bumann, D., Lubitz, W., and Möbius, K. (1990) ENDOR and TRIPLE resonance investigation of the primary donor cation radical P865 in single crystals of Rhodobacter sphaeroides R-26 reaction centers, in Reaction Centers of Photosynthetic Bacteria (Michel-Beyerle, M. E., Ed.) pp 57-68, Springer-Verlag, Berlin.
    • (1990) Reaction Centers of Photosynthetic Bacteria , pp. 57-68
    • Lendzian, F.1    Endeward, B.2    Plato, M.3    Bumann, D.4    Lubitz, W.5    Möbius, K.6
  • 37
    • 1642412610 scopus 로고    scopus 로고
    • Hydrogen bond geometries from electron paramagnetic resonance and electron-nuclear double resonance parameters: Density functional study of quinone radical anion-solvent interactions
    • Sinnecker, S., Reijerse, E., Neese, F., and Lubitz, W. (2004) Hydrogen bond geometries from electron paramagnetic resonance and electron-nuclear double resonance parameters: Density functional study of quinone radical anion-solvent interactions, J. Am. Chem. Soc. 126, 3280-3290.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 3280-3290
    • Sinnecker, S.1    Reijerse, E.2    Neese, F.3    Lubitz, W.4
  • 40
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction-center from Rhodobacter sphaeroides at 2.65-angstrom resolution - cofactors and protein-cofactor interactions
    • Ermler, U., Fritzsch, G., Buchanan, S. K., and Michel, H. (1994) Structure of the photosynthetic reaction-center from Rhodobacter sphaeroides at 2.65-angstrom resolution - cofactors and protein-cofactor interactions, Structure 2, 925-936.
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 41
    • 36549101162 scopus 로고
    • Analysis of N-14 Eseem patterns of randomly oriented solids
    • Flanagan, H. L., and Singel, D. J. (1987) Analysis of N-14 Eseem patterns of randomly oriented solids, J. Chem. Phys. 87, 5606-5616.
    • (1987) J. Chem. Phys , vol.87 , pp. 5606-5616
    • Flanagan, H.L.1    Singel, D.J.2
  • 43
    • 0019003786 scopus 로고
    • Pulsed electron-paramagnetic resonance studies of the copper(II) site in galactose-oxidase
    • Kosman, D. J., Peisach, J., and Mims, W. B. (1980) Pulsed electron-paramagnetic resonance studies of the copper(II) site in galactose-oxidase, Biochemistry 19, 1304-1308.
    • (1980) Biochemistry , vol.19 , pp. 1304-1308
    • Kosman, D.J.1    Peisach, J.2    Mims, W.B.3
  • 44
    • 0019332726 scopus 로고
    • Electron-spin echo studies of cytochrome-c oxidase
    • Mims, W. B., Peisach, J., Shaw, R. W., and Beinert, H. (1980) Electron-spin echo studies of cytochrome-c oxidase, J. Biol. Chem. 255, 6843-6846.
    • (1980) J. Biol. Chem , vol.255 , pp. 6843-6846
    • Mims, W.B.1    Peisach, J.2    Shaw, R.W.3    Beinert, H.4
  • 45
    • 0017083127 scopus 로고
    • Assignment of a ligand in stellacyanin by a pulsed electron-paramagnetic resonance method
    • Mims, W. B., and Peisach, J. (1976) Assignment of a ligand in stellacyanin by a pulsed electron-paramagnetic resonance method, Biochemistry 15, 3863-3869.
    • (1976) Biochemistry , vol.15 , pp. 3863-3869
    • Mims, W.B.1    Peisach, J.2
  • 46
    • 0017657490 scopus 로고
    • Pulsed electron-paramagnetic resonance studies of types-I and type-Ii copper of Rhus-Vernicifera laccase and porcine ceruloplasmin
    • Mondovi, B., Graziani, M. T., Mims, W. B., Oltzik, R., and Peisach, J. (1977) Pulsed electron-paramagnetic resonance studies of types-I and type-Ii copper of Rhus-Vernicifera laccase and porcine ceruloplasmin, Biochemistry 16, 4198-4202.
    • (1977) Biochemistry , vol.16 , pp. 4198-4202
    • Mondovi, B.1    Graziani, M.T.2    Mims, W.B.3    Oltzik, R.4    Peisach, J.5
  • 47
    • 37349013310 scopus 로고
    • Electron-spin echo envelope modulation (Eseem) spectroscopy of the triplet-state of the primary donor of N-14 and N-15 bacterial photosynthetic reaction centers and of N-14 and N-15 bacteriochlorophyll-A
    • de Groot, A., Evelo, R., Hoff, A. J., de Beer, R., and Scheer, H. (1985) Electron-spin echo envelope modulation (Eseem) spectroscopy of the triplet-state of the primary donor of N-14 and N-15 bacterial photosynthetic reaction centers and of N-14 and N-15 bacteriochlorophyll-A, Chem. Phys. Lett. 118, 48-54.
    • (1985) Chem. Phys. Lett , vol.118 , pp. 48-54
    • de Groot, A.1    Evelo, R.2    Hoff, A.J.3    de Beer, R.4    Scheer, H.5
  • 48
    • 0035528067 scopus 로고    scopus 로고
    • A D-band (130 GHz) EPR study of the primary electron donor triplet state in photosynthetic reaction centers of Rhodobacter sphaeroides R-26
    • Paschenko, S. V., Gast, P., and Hoff, A. J. (2001) A D-band (130 GHz) EPR study of the primary electron donor triplet state in photosynthetic reaction centers of Rhodobacter sphaeroides R-26, Appl. Magn. Reson. 21, 325-334.
    • (2001) Appl. Magn. Reson , vol.21 , pp. 325-334
    • Paschenko, S.V.1    Gast, P.2    Hoff, A.J.3
  • 49
    • 0035528073 scopus 로고    scopus 로고
    • The g-tensor anisotropy of the triplet state of the primary electron donor in the photosynthetic bacterium Rhodobacter sphaeroides by high-field (95 GHz) EPR
    • Labahn, A., and Huber, M. (2001) The g-tensor anisotropy of the triplet state of the primary electron donor in the photosynthetic bacterium Rhodobacter sphaeroides by high-field (95 GHz) EPR, Appl. Magn. Reson. 21, 381-387.
    • (2001) Appl. Magn. Reson , vol.21 , pp. 381-387
    • Labahn, A.1    Huber, M.2
  • 50
    • 33746903125 scopus 로고    scopus 로고
    • Importance of direct spin-spin coupling and spin-flip excitations for the zero-field splittings of transition metal complexes: A case study
    • Neese, F. (2006) Importance of direct spin-spin coupling and spin-flip excitations for the zero-field splittings of transition metal complexes: A case study, J. Am. Chem. Soc. 128, 10213-10222.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 10213-10222
    • Neese, F.1
  • 51
    • 0030294712 scopus 로고    scopus 로고
    • Triplet state energy transfer between the primary donor and the carotenoid in Rhodobacter sphaeroides R-26.1 reaction centers exchanged with modified bacteriochlorophyll pigments and reconstituted with spheroidene
    • Frank, H. A., Chynwat, V., Posteraro, A., Hartwich, G., Simonin, I., and Scheer, H. (1996) Triplet state energy transfer between the primary donor and the carotenoid in Rhodobacter sphaeroides R-26.1 reaction centers exchanged with modified bacteriochlorophyll pigments and reconstituted with spheroidene, Photochem. Photobiol. 64, 823-831.
    • (1996) Photochem. Photobiol , vol.64 , pp. 823-831
    • Frank, H.A.1    Chynwat, V.2    Posteraro, A.3    Hartwich, G.4    Simonin, I.5    Scheer, H.6
  • 52
    • 33144475803 scopus 로고    scopus 로고
    • Triplet-state conformational changes in 15-cis-spheroidene bound to the reaction center from Rhodobacter sphaeroides 2.4.1 as revealed by time-resolved EPR spectroscopy: Strengthened hypothetical mechanism of triplet-energy dissipation
    • Kakitani, Y., Fujii, R., Koyama, Y., Nagae, H., Walker, L., Salter, B., and Angerhofer, A. (2006) Triplet-state conformational changes in 15-cis-spheroidene bound to the reaction center from Rhodobacter sphaeroides 2.4.1 as revealed by time-resolved EPR spectroscopy: Strengthened hypothetical mechanism of triplet-energy dissipation, Biochemistry 45, 2053-2062.
    • (2006) Biochemistry , vol.45 , pp. 2053-2062
    • Kakitani, Y.1    Fujii, R.2    Koyama, Y.3    Nagae, H.4    Walker, L.5    Salter, B.6    Angerhofer, A.7
  • 54
    • 0031980123 scopus 로고    scopus 로고
    • Protein modifications affecting triplet energy transfer in bacterial photosynthetic reaction centers
    • Laible, P. D., Chynwat, V., Thurnauer, M. C., Schiffer, M., Hanson, D. K., and Frank, H. A. (1998) Protein modifications affecting triplet energy transfer in bacterial photosynthetic reaction centers, Biophys. J. 74, 2623-2637.
    • (1998) Biophys. J , vol.74 , pp. 2623-2637
    • Laible, P.D.1    Chynwat, V.2    Thurnauer, M.C.3    Schiffer, M.4    Hanson, D.K.5    Frank, H.A.6
  • 55
    • 0027420706 scopus 로고
    • A monomeric bacteriochlorophyll triplet-state ((3)B) in reaction centers of Rhodobacter sphaeroides R-26, studied by absorption-detected magnetic-resonance
    • Angerhofer, A., and Aust, V. (1993) A monomeric bacteriochlorophyll triplet-state ((3)B) in reaction centers of Rhodobacter sphaeroides R-26, studied by absorption-detected magnetic-resonance, J. Photochem. Photobiol., B 20, 127-132.
    • (1993) J. Photochem. Photobiol., B , vol.20 , pp. 127-132
    • Angerhofer, A.1    Aust, V.2
  • 56
    • 0029164356 scopus 로고
    • Absorption and Admr studies on bacterial photosynthetic reaction centers with modified pigments
    • Hartwich, G., Scheer, H., Aust, V., and Angerhofer, A. (1995) Absorption and Admr studies on bacterial photosynthetic reaction centers with modified pigments, Biochim. Biophys. Acta 1230, 97-113.
    • (1995) Biochim. Biophys. Acta , vol.1230 , pp. 97-113
    • Hartwich, G.1    Scheer, H.2    Aust, V.3    Angerhofer, A.4
  • 57
    • 0017178846 scopus 로고
    • Kinetics of populating and depopulating of components of photoinduced triplet-state of photosynthetic bacteria Rhodospirillum rubrum, Rhodopseudomonas spheroides (wild-type), and its mutant R-26 as measured by ESR in zero-field
    • Hoff, A. J. (1976) Kinetics of populating and depopulating of components of photoinduced triplet-state of photosynthetic bacteria Rhodospirillum rubrum, Rhodopseudomonas spheroides (wild-type), and its mutant R-26 as measured by ESR in zero-field, Biochim. Biophys. Acta 440, 765-771.
    • (1976) Biochim. Biophys. Acta , vol.440 , pp. 765-771
    • Hoff, A.J.1
  • 59
    • 24244435109 scopus 로고
    • Position-dependent deuterium effect on relative rate constants for Isc processes in aromatic-hydrocarbons
    • Metz, F. (1973) Position-dependent deuterium effect on relative rate constants for Isc processes in aromatic-hydrocarbons, Chem. Phys. Lett. 22, 186-190.
    • (1973) Chem. Phys. Lett , vol.22 , pp. 186-190
    • Metz, F.1
  • 60
    • 0017151974 scopus 로고
    • Triplet-states of bacteriochlorophyll and carotenoids in chromatophores of photosynthetic bacteria
    • Monger, T. G., Cogdell, R. J., and Parson, W. W. (1976) Triplet-states of bacteriochlorophyll and carotenoids in chromatophores of photosynthetic bacteria, Biochim. Biophys. Acta 449, 136-153.
    • (1976) Biochim. Biophys. Acta , vol.449 , pp. 136-153
    • Monger, T.G.1    Cogdell, R.J.2    Parson, W.W.3
  • 61
    • 0000328769 scopus 로고
    • Time-resolved Epr of the radical pair P(865)(+)Q(A)-(-) in bacterial reaction centers - observation of transient nutations, quantum beats and envelope modulation effects
    • Bittl, R., van der Est, A., Kamlowski, A., Lubitz, W., and Stehlik, D. (1994) Time-resolved Epr of the radical pair P(865)(+)Q(A)-(-) in bacterial reaction centers - observation of transient nutations, quantum beats and envelope modulation effects, Chem. Phys. Lett. 226, 349-358.
    • (1994) Chem. Phys. Lett , vol.226 , pp. 349-358
    • Bittl, R.1    van der Est, A.2    Kamlowski, A.3    Lubitz, W.4    Stehlik, D.5
  • 62
    • 0024975267 scopus 로고
    • Structure of spheroidene in the photosynthetic reaction center from Y-Rhodobacter-sphaeroides
    • Arnoux, B., Ducruix, A., Reisshusson, F., Lutz, M., Norris, J., Schiffer, M., and Chang, C. H. (1989) Structure of spheroidene in the photosynthetic reaction center from Y-Rhodobacter-sphaeroides, FEBS Lett. 258, 47-50.
    • (1989) FEBS Lett , vol.258 , pp. 47-50
    • Arnoux, B.1    Ducruix, A.2    Reisshusson, F.3    Lutz, M.4    Norris, J.5    Schiffer, M.6    Chang, C.H.7
  • 63
    • 0003693731 scopus 로고
    • Blankenship, R, Madigan, M, and Bauer, C, Eds, Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Woodbury, N., and Allen, J. (1995) in Anoxygenic Photosynthetic Bacteria (Blankenship, R., Madigan, M., and Bauer, C., Eds.) Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria
    • Woodbury, N.1    Allen, J.2
  • 64
    • 0024355943 scopus 로고
    • A superexchange mechanism for the primary charge separation in photosynthetic reaction centers
    • Bixon, M., Jortner, J., Michel-Beyerle, M. E., and Ogrodnik, A. (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
  • 65
    • 4243799735 scopus 로고
    • Reflectance spectrum and electronic states of CuCl ion in a number of crystal lattices
    • Allen, G. C., and Hush, N. S. (1967) Reflectance spectrum and electronic states of CuCl ion in a number of crystal lattices, Inorg. Chem. 6, 4-15.
    • (1967) Inorg. Chem , vol.6 , pp. 4-15
    • Allen, G.C.1    Hush, N.S.2
  • 66
    • 0000524441 scopus 로고    scopus 로고
    • A chemical approach towards the photosynthetic reaction center
    • Osuka, A., Mataga, N., and Okada, T. (1997) A chemical approach towards the photosynthetic reaction center, Pure Appl. Chem. 69, 797-802.
    • (1997) Pure Appl. Chem , vol.69 , pp. 797-802
    • Osuka, A.1    Mataga, N.2    Okada, T.3
  • 67
    • 1842555190 scopus 로고    scopus 로고
    • Unified description of the electrochemical, charge distribution, and spectroscopic properties of the special-pair radical cation in bacterial photosynthesis
    • Reimers, J. R., and Hush, N. S. (2004) Unified description of the electrochemical, charge distribution, and spectroscopic properties of the special-pair radical cation in bacterial photosynthesis, J. Am. Chem. Soc. 126, 4132-4144.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 4132-4144
    • Reimers, J.R.1    Hush, N.S.2
  • 68
    • 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
    • Breton, J., Nabedryk, E., and Parson, W. W. (1992) 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, 7503-7510.
    • (1992) Biochemistry , vol.31 , pp. 7503-7510
    • Breton, J.1    Nabedryk, E.2    Parson, W.W.3


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