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Volumn 44, Issue 20, 2005, Pages 7389-7394

Design of a redox-linked active metal site: Manganese bound to bacterial reaction centers at a site resembling that of photosystem II

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CHLOROPHYLL; DISSOCIATION; OXIDATION; PROTEINS; X RAY DIFFRACTION ANALYSIS;

EID: 18844438921     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050377n     Document Type: Article
Times cited : (56)

References (29)
  • 2
    • 0028000028 scopus 로고
    • Specific alteration of the oxidation potential of the electron donor in reaction centers from Rhodobacter sphaeroides
    • Lin, X., Murchinson, H. A., Nagarajan, V., Parson, W. W., Allen, J. P., and Williams, J. C. (1994) Specific alteration of the oxidation potential of the electron donor in reaction centers from Rhodobacter sphaeroides, Proc. Natl. Acad. Sci. U.S.A. 91, 10265-10269.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 10265-10269
    • Lin, X.1    Murchinson, H.A.2    Nagarajan, V.3    Parson, W.W.4    Allen, J.P.5    Williams, J.C.6
  • 3
    • 0038816843 scopus 로고    scopus 로고
    • Modified reaction centres oxidize tyrosine in reactions that mirror photosystem II
    • Kálmán, L., LoBrutto, R., Allen, J. P., and Williams, J. C. (1999) Modified reaction centres oxidize tyrosine in reactions that mirror photosystem II, Nature 402, 696-699.
    • (1999) Nature , vol.402 , pp. 696-699
    • Kálmán, L.1    LoBrutto, R.2    Allen, J.P.3    Williams, J.C.4
  • 4
    • 0141542722 scopus 로고    scopus 로고
    • Manganese oxidation by modified reaction centers from Rhodobacter sphaeroides
    • Kálmán, L., LoBrutto, R., Allen, J. P., and Williams, J. C. (2003) Manganese oxidation by modified reaction centers from Rhodobacter sphaeroides, Biochemistry 42, 11016-11022.
    • (2003) Biochemistry , vol.42 , pp. 11016-11022
    • Kálmán, L.1    LoBrutto, R.2    Allen, J.P.3    Williams, J.C.4
  • 6
    • 0031473227 scopus 로고    scopus 로고
    • Structural chemistry and biology of manganese metalloenzymes
    • Christianson, D. W. (1997) Structural chemistry and biology of manganese metalloenzymes, Prog. Biophys. Mol. Biol. 67, 217-252.
    • (1997) Prog. Biophys. Mol. Biol. , vol.67 , pp. 217-252
    • Christianson, D.W.1
  • 7
    • 0035808668 scopus 로고    scopus 로고
    • 4-cluster of photosynthetic oxygen evolving complex
    • 4-cluster of photosynthetic oxygen evolving complex, Biochim. Biophys. Acta 1503, 40-51.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 40-51
    • Ono, T.1
  • 8
    • 0035808665 scopus 로고    scopus 로고
    • Z and the manganese cluster in the water oxidizing complex of photosystem II
    • Z and the manganese cluster in the water oxidizing complex of photosystem II, Biochim. Biophys. Acta 1503, 164-186.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 164-186
    • Debus, R.J.1
  • 9
    • 0035808702 scopus 로고    scopus 로고
    • Amino acid residues involved in the coordination and assembly of the manganese cluster of photosystem II. Proton-coupled electron transport of the redox-active tyrosines and its relationship to water oxidation
    • Diner, B. A. (2001) Amino acid residues involved in the coordination and assembly of the manganese cluster of photosystem II. Proton-coupled electron transport of the redox-active tyrosines and its relationship to water oxidation, Biochim. Biophys. Acta 1503, 147-163.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 147-163
    • Diner, B.A.1
  • 10
    • 0043145962 scopus 로고
    • Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II
    • Michel, H., and Deisenhofer, J. (1988) Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II, Biochemistry 27, 1-7.
    • (1988) Biochemistry , vol.27 , pp. 1-7
    • Michel, H.1    Deisenhofer, J.2
  • 11
    • 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., Yeates, T. O., Rees, D. C., Allen, J. P., and Feher, G. (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. U.S.A. 85, 9012-9016.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 9012-9016
    • Komiya, H.1    Yeates, T.O.2    Rees, D.C.3    Allen, J.P.4    Feher, G.5
  • 12
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • Zouni, A., Witt, H. T., Kern, J., Fromme, P., Krauss, N., Saenger, W., and Orth, P. (2001) Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution, Nature 409, 739-743.
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7
  • 13
    • 0026442123 scopus 로고
    • Effects of mutations near the bacteriochlorophylls in reaction centers from Rhodobacter sphaeroides
    • Williams, J. C., Alden, R. G., Murchison, H. A., Peloquin, J. M., Woodbury, N. W., and Allen, J. P. (1992) Effects of mutations near the bacteriochlorophylls in reaction centers from Rhodobacter sphaeroides, Biochemistry 31, 11029-11037.
    • (1992) Biochemistry , vol.31 , pp. 11029-11037
    • Williams, J.C.1    Alden, R.G.2    Murchison, H.A.3    Peloquin, J.M.4    Woodbury, N.W.5    Allen, J.P.6
  • 14
    • 0000552904 scopus 로고
    • Genetic Manipulation of Purple Photosynthetic Bacteria
    • Blankenship, R. E., Madigan, M. T., and Bauer, C. E., Eds. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Williams, J. C., and Taguchi, A. K. W. (1995) Genetic Manipulation of Purple Photosynthetic Bacteria, in Anoxygenic Photosynthetic Bacteria (Blankenship, R. E., Madigan, M. T., and Bauer, C. E., Eds.) pp 1029-1065 Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 1029-1065
    • Williams, J.C.1    Taguchi, A.K.W.2
  • 15
    • 0024726467 scopus 로고
    • Pathway of proton transfer in bacterial reaction centers: Replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover
    • Paddock, M. L., Rongey, S. H., Feher, G., and Okamura, M. Y. (1989) Pathway of proton transfer in bacterial reaction centers: Replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover, Proc. Natl. Acad. Sci. U.S.A. 86, 6602-6606.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 6602-6606
    • Paddock, M.L.1    Rongey, S.H.2    Feher, G.3    Okamura, M.Y.4
  • 16
  • 17
    • 0028474518 scopus 로고
    • Spectroscopic evidence for the presence of an iron-sulfur center similar to FX of photosystem I in Heliobacillus mobilis
    • Kleinherenbrink, F. A. M., Chiou, H. C., LoBrutto, R., and Blankenship, R. E. (1994) Spectroscopic evidence for the presence of an iron-sulfur center similar to FX of photosystem I in Heliobacillus mobilis, Photosynth. Res. 41, 115-123.
    • (1994) Photosynth. Res. , vol.41 , pp. 115-123
    • Kleinherenbrink, F.A.M.1    Chiou, H.C.2    LoBrutto, R.3    Blankenship, R.E.4
  • 18
    • 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
  • 19
    • 0033212815 scopus 로고    scopus 로고
    • Integration of macromolecular diffraction data
    • Leslie, A. G. W. (1999) Integration of macromolecular diffraction data, Acta Crystallogr. D55, 1696-1702.
    • (1999) Acta Crystallogr. , vol.D55 , pp. 1696-1702
    • Leslie, A.G.W.1
  • 20
    • 0037143641 scopus 로고    scopus 로고
    • Interactions between lipids and bacterial reaction centers determined by protein crystallography
    • Cámara-Artigas, A., Brune, D., and Allen, J. P. (2002) Interactions between lipids and bacterial reaction centers determined by protein crystallography, Proc. Natl. Acad. Sci. U.S.A. 99, 11055-11060.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11055-11060
    • Cámara-Artigas, A.1    Brune, D.2    Allen, J.P.3
  • 21
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for Protein Crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 Suite: Programs for Protein Crystallography, Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 22
    • 0030864522 scopus 로고    scopus 로고
    • Crystallographic refinement by simulated annealing: Methods and applications
    • Brunger, A. T., and Rice, L. M. (1997) Crystallographic refinement by simulated annealing: Methods and applications, Methods Enzymol. 277, 243-269.
    • (1997) Methods Enzymol. , vol.277 , pp. 243-269
    • Brunger, A.T.1    Rice, L.M.2
  • 23
    • 4944231214 scopus 로고    scopus 로고
    • Dependence of tyrosine oxidation in highly oxidizing bacterial reaction centers on pH and free-energy difference
    • Kálmán, L., Narváez, A. J., LoBrutto, R., Williams, J. C., and Allen, J. P. (2004) Dependence of tyrosine oxidation in highly oxidizing bacterial reaction centers on pH and free-energy difference, Biochemistry 43, 12905-12912.
    • (2004) Biochemistry , vol.43 , pp. 12905-12912
    • Kálmán, L.1    Narváez, A.J.2    LoBrutto, R.3    Williams, J.C.4    Allen, J.P.5
  • 24
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page, C. C., Moser, C. C., Chen, X., and Dutton, P. L. (1999) Natural engineering principles of electron tunnelling in biological oxidation-reduction, Nature 402, 47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 25
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the photosynthetic oxygen-evolving center
    • Ferreira, K. N., Iverson, T. M., Maghlaoui, K., Barber, J., and Iwata, S. (2004) Architecture of the photosynthetic oxygen-evolving center, Science 303, 1831-1838.
    • (2004) Science , vol.303 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 26
    • 0032031956 scopus 로고    scopus 로고
    • The origin and evolution of oxygenic photosynthesis
    • Blankenship, R. E., and Hartman, H. (1998) The origin and evolution of oxygenic photosynthesis, Trends Biochem. Sci. 23, 94-97.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 94-97
    • Blankenship, R.E.1    Hartman, H.2
  • 27
    • 0037150088 scopus 로고    scopus 로고
    • Electrostatic interactions in an integral membrane protein
    • Johnson, E. T., and Parson, W. W. (2002) Electrostatic interactions in an integral membrane protein, Biochemistry 41, 6483-6494.
    • (2002) Biochemistry , vol.41 , pp. 6483-6494
    • Johnson, E.T.1    Parson, W.W.2
  • 29
    • 0041428115 scopus 로고    scopus 로고
    • Designing redox metalloproteins from bottom-up and top-down perspectives
    • Barker, P. D. (2003) Designing redox metalloproteins from bottom-up and top-down perspectives, Curr. Opin. Struct. Biol. 13, 490-499.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 490-499
    • Barker, P.D.1


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