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Volumn 368, Issue 1, 2007, Pages 197-208

A Comparison of Stigmatellin Conformations, Free and Bound to the Photosynthetic Reaction Center and the Cytochrome bc1 Complex

Author keywords

conformational energy; electron transfer; inhibitor; membrane protein complexes; X ray crystal structures

Indexed keywords

MEMBRANE PROTEIN; STIGMATELLIN; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 33947302684     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.02.013     Document Type: Article
Times cited : (42)

References (39)
  • 1
    • 45149142322 scopus 로고
    • The discovery of coenzyme Q. A commentary on isolation of a quinone from beef heart mitochondria
    • Crane F.L. The discovery of coenzyme Q. A commentary on isolation of a quinone from beef heart mitochondria. Biochim. Biophys. Acta 1000 (1989) 358-363
    • (1989) Biochim. Biophys. Acta , vol.1000 , pp. 358-363
    • Crane, F.L.1
  • 3
    • 33947301118 scopus 로고    scopus 로고
    • Purple bacteria: photosynthetic reaction centers
    • Lennarz W.J., and Lane M.D. (Eds), Elsevier Science Inc, New York
    • Lancaster C.R.D. Purple bacteria: photosynthetic reaction centers. In: Lennarz W.J., and Lane M.D. (Eds). Encyclopedia of Biological Chemistry (2004), Elsevier Science Inc, New York 586-594
    • (2004) Encyclopedia of Biological Chemistry , pp. 586-594
    • Lancaster, C.R.D.1
  • 4
    • 33947302849 scopus 로고    scopus 로고
    • 1 complex (respiratory chain complex III)
    • Lennarz W.J., and Lane M.D. (Eds), Elsevier Science Inc., New York
    • 1 complex (respiratory chain complex III). In: Lennarz W.J., and Lane M.D. (Eds). Encyclopedia of Biological Chemistry (2004), Elsevier Science Inc., New York 528-534
    • (2004) Encyclopedia of Biological Chemistry , pp. 528-534
    • Trumpower, B.L.1
  • 5
    • 0017148721 scopus 로고
    • Possible mechanisms of protonmotive function of cytochrome systems
    • Mitchell P. Possible mechanisms of protonmotive function of cytochrome systems. J. Theor. Biol. 62 (1976) 327-367
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 6
    • 84961475117 scopus 로고
    • Herbicide and quinone binding to chromatophores and reaction centers from Rhodobacter sphaeroides
    • Oettmeier W., and Preuße S. Herbicide and quinone binding to chromatophores and reaction centers from Rhodobacter sphaeroides. Z. Naturforsch. 42c (1987) 690-692
    • (1987) Z. Naturforsch. , vol.42 c , pp. 690-692
    • Oettmeier, W.1    Preuße, S.2
  • 8
    • 0000194606 scopus 로고
    • Stigmatellin. A dual type inhibitor of photosynthetic electron transport
    • Oettmeier W., Godde D., Kunze B., and Höfle G. Stigmatellin. A dual type inhibitor of photosynthetic electron transport. Biochim. Biophys. Acta 807 (1985) 216-219
    • (1985) Biochim. Biophys. Acta , vol.807 , pp. 216-219
    • Oettmeier, W.1    Godde, D.2    Kunze, B.3    Höfle, G.4
  • 11
    • 0021273146 scopus 로고
    • Stigmatellin, a new antibiotic from Stigmatella aurantiaca (Myxobacterales) I. Production, physico-chemical and biological properties
    • Kunze B., Kemmer T., Hofle G., and Reichenbach H. Stigmatellin, a new antibiotic from Stigmatella aurantiaca (Myxobacterales) I. Production, physico-chemical and biological properties. J. Antibiot. 37 (1984) 454-461
    • (1984) J. Antibiot. , vol.37 , pp. 454-461
    • Kunze, B.1    Kemmer, T.2    Hofle, G.3    Reichenbach, H.4
  • 12
    • 0034647038 scopus 로고    scopus 로고
    • Diastereo- and enantioselective total synthesis of stigmatellin A
    • Enders D., Geibel G., and Osboren S. Diastereo- and enantioselective total synthesis of stigmatellin A. Chem. Eur. J. 6 (2000) 1302-1309
    • (2000) Chem. Eur. J. , vol.6 , pp. 1302-1309
    • Enders, D.1    Geibel, G.2    Osboren, S.3
  • 14
    • 0034660152 scopus 로고    scopus 로고
    • 1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment
    • 1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Structure 8 (2000) 669-684
    • (2000) Structure , vol.8 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Roßmanith, T.4    Michel, H.5
  • 16
    • 22544467474 scopus 로고    scopus 로고
    • 1 complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern
    • 1 complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern. J. Mol. Biol. 351 (2005) 573-597
    • (2005) J. Mol. Biol. , vol.351 , pp. 573-597
    • Huang, L.S.1    Cobessi, D.2    Tung, E.Y.3    Berry, E.A.4
  • 20
    • 0000999832 scopus 로고
    • The{combining comma below} light' and{combining comma below} medium' subunits of the photosynthetic reaction centre from Rhodopseudomonas viridis: isolation of the genes, nucleotide and amino acid sequence
    • Michel H., Weyer K.A., Gruenberg H., Dunger I., Oesterhelt D., and Lottspeich F. The{combining comma below} light' and{combining comma below} medium' subunits of the photosynthetic reaction centre from Rhodopseudomonas viridis: isolation of the genes, nucleotide and amino acid sequence. EMBO J. 5 (1986) 1149-1158
    • (1986) EMBO J. , vol.5 , pp. 1149-1158
    • Michel, H.1    Weyer, K.A.2    Gruenberg, H.3    Dunger, I.4    Oesterhelt, D.5    Lottspeich, F.6
  • 21
    • 0005384356 scopus 로고
    • The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis
    • Deisenhofer J., and Michel H. The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis. EMBO J. 8 (1989) 2149-2170
    • (1989) EMBO J. , vol.8 , pp. 2149-2170
    • Deisenhofer, J.1    Michel, H.2
  • 22
    • 0012764703 scopus 로고    scopus 로고
    • Photosynthetic reaction centers of purple bacteria
    • Wieghardt K., Huber R., Poulos T., and Messerschmidt A. (Eds), Wiley, Chichester
    • Lancaster C.R.D., and Michel H. Photosynthetic reaction centers of purple bacteria. In: Wieghardt K., Huber R., Poulos T., and Messerschmidt A. (Eds). Handbook of Metalloproteins vol. 1 (2001), Wiley, Chichester 119-135
    • (2001) Handbook of Metalloproteins , vol.1 , pp. 119-135
    • Lancaster, C.R.D.1    Michel, H.2
  • 24
    • 0347170005 scopus 로고
    • Self-consistent molecular orbital methods. XII. Further extensions of Gaussian-type basis sets for use in molecular orbital studies of organic molecules
    • Hehre W.J., Ditchfield R., and Pople J.A. Self-consistent molecular orbital methods. XII. Further extensions of Gaussian-type basis sets for use in molecular orbital studies of organic molecules. J. Chem. Phys. 56 (1972) 2257-2261
    • (1972) J. Chem. Phys. , vol.56 , pp. 2257-2261
    • Hehre, W.J.1    Ditchfield, R.2    Pople, J.A.3
  • 25
    • 49649133169 scopus 로고
    • Effect of d-functions on molecular orbital energies for hydrocarbons
    • Hariharan P.C., and Pople J.A. Effect of d-functions on molecular orbital energies for hydrocarbons. Chem. Phys. Letters 66 (1972) 217-219
    • (1972) Chem. Phys. Letters , vol.66 , pp. 217-219
    • Hariharan, P.C.1    Pople, J.A.2
  • 26
    • 84988115618 scopus 로고
    • Validation of the general purpose tripos 5.2 force field
    • Clark M., Cramer III R.D., and van Opdenbosch N. Validation of the general purpose tripos 5.2 force field. J. Comput. Chem. 10 (1989) 982-1012
    • (1989) J. Comput. Chem. , vol.10 , pp. 982-1012
    • Clark, M.1    Cramer III, R.D.2    van Opdenbosch, N.3
  • 27
    • 0034671487 scopus 로고    scopus 로고
    • Structural basis of the drastically increased initial electron transfer rate in a reaction center from Rhodopseudomonas viridis mutant described at 2.00 Å resolution
    • Lancaster C.R.D., Bibikova M.V., Sabatino P., Oesterhelt D., and Michel H. Structural basis of the drastically increased initial electron transfer rate in a reaction center from Rhodopseudomonas viridis mutant described at 2.00 Å resolution. J. Biol. Chem. 275 (2000) 39364-39368
    • (2000) J. Biol. Chem. , vol.275 , pp. 39364-39368
    • Lancaster, C.R.D.1    Bibikova, M.V.2    Sabatino, P.3    Oesterhelt, D.4    Michel, H.5
  • 28
    • 0033605220 scopus 로고    scopus 로고
    • Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid
    • Lancaster C.R.D., and Michel H. Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid. J. Mol. Biol. 286 (1999) 883-898
    • (1999) J. Mol. Biol. , vol.286 , pp. 883-898
    • Lancaster, C.R.D.1    Michel, H.2
  • 29
    • 0037059734 scopus 로고    scopus 로고
    • 1 complex. Evidence for an alternating, half-of-the-sites mechanism of ubiquinol oxidation
    • 1 complex. Evidence for an alternating, half-of-the-sites mechanism of ubiquinol oxidation. J. Biol. Chem. 277 (2002) 1195-1202
    • (2002) J. Biol. Chem. , vol.277 , pp. 1195-1202
    • Gutierrez-Cirlos, E.B.1    Trumpower, B.L.2
  • 30
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer
    • Stowell M.H., McPhillips T.M., Rees D.C., Soltis S.M., Abresch E., and Feher G. Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Science 276 (1997) 812-816
    • (1997) Science , vol.276 , pp. 812-816
    • Stowell, M.H.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 31
    • 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. Charge separation induces conformational changes in the photosynthetic reaction centre of purple bacteria. Acta Crystallog. sect. D 58 (2002) 1660-1663
    • (2002) Acta Crystallog. sect. D , vol.58 , pp. 1660-1663
    • Fritzsch, G.1    Koepke, J.2    Diem, R.3    Kuglstatter, A.4    Baciou, L.5
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0031022026 scopus 로고    scopus 로고
    • Transfer of the bacteriochlorophyll b-containing phototrophic bacteria Rhodopseudomonas viridis and Rhodopseudomonas sulfoviridis to the genus Blastochloris gen nov
    • Hiraishi A. Transfer of the bacteriochlorophyll b-containing phototrophic bacteria Rhodopseudomonas viridis and Rhodopseudomonas sulfoviridis to the genus Blastochloris gen nov. Int. J. Syst. Bacteriol. 47 (1997) 217-219
    • (1997) Int. J. Syst. Bacteriol. , vol.47 , pp. 217-219
    • Hiraishi, A.1
  • 37
    • 0026597444 scopus 로고
    • Free R-value - a novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A.T. Free R-value - a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355 (1992) 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 38
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati P.V. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5 (1952) 802-810
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, P.V.1
  • 39
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R.A., and Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A 47 (1991) 392-400
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.