메뉴 건너뛰기




Volumn 180, Issue 2, 2006, Pages 178-185

Distance between a native cofactor and a spin label in the reaction centre of Rhodobacter sphaeroides by a two-frequency pulsed electron paramagnetic resonance method and molecular dynamics simulations

Author keywords

Distance determination; Double electron electron resonance; Molecular dynamics simulations; Reaction centre Rhodobacter sphaeroides; Spin label EPR

Indexed keywords

CHEMICAL REACTIONS; COMPUTER SIMULATION; MOLECULAR DYNAMICS; NEGATIVE IONS; PHOTOSYNTHESIS; PROTEINS;

EID: 33646379349     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2006.02.008     Document Type: Article
Times cited : (41)

References (25)
  • 1
    • 0021674417 scopus 로고
    • Electron-transfer 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. Electron-transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state-evidence for light-induced structural-changes. Biochemistry 23 (1984) 5780-5786
    • (1984) Biochemistry , vol.23 , pp. 5780-5786
    • Kleinfeld, D.1    Okamura, M.Y.2    Feher, G.3
  • 2
    • 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. 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.B.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 3
    • 0038079688 scopus 로고    scopus 로고
    • Probing local dynamics of the photosynthetic bacterial reaction center with a cysteine specific spin label
    • Poluektov O.G., Utschig L.M., Dalosto S., and Thurnauer M.C. Probing local dynamics of the photosynthetic bacterial reaction center with a cysteine specific spin label. J. Phys. Chem. B 107 (2003) 6239-6244
    • (2003) J. Phys. Chem. B , vol.107 , pp. 6239-6244
    • Poluektov, O.G.1    Utschig, L.M.2    Dalosto, S.3    Thurnauer, M.C.4
  • 4
    • 21644446664 scopus 로고    scopus 로고
    • Explicit treatment of spin labels in modeling of distance constraints from dipolar EPR and DEER
    • Sale K., Song L.K., Liu Y.S., Perozo E., and Fajer P. Explicit treatment of spin labels in modeling of distance constraints from dipolar EPR and DEER. J. Am. Chem. Soc. 127 (2005) 9334-9335
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 9334-9335
    • Sale, K.1    Song, L.K.2    Liu, Y.S.3    Perozo, E.4    Fajer, P.5
  • 5
    • 0036290220 scopus 로고    scopus 로고
    • Direct conversion of EPR dipolar time evolution data to distance distributions
    • Jeschke G., Koch A., Jonas U., and Godt A. Direct conversion of EPR dipolar time evolution data to distance distributions. J. Magn. Reson. 155 (2002) 72-82
    • (2002) J. Magn. Reson. , vol.155 , pp. 72-82
    • Jeschke, G.1    Koch, A.2    Jonas, U.3    Godt, A.4
  • 6
    • 0037112592 scopus 로고    scopus 로고
    • Distance measurements in the nanometer range by pulse EPR
    • Jeschke G. Distance measurements in the nanometer range by pulse EPR. Chemphyschem 3 (2002) 927-932
    • (2002) Chemphyschem , vol.3 , pp. 927-932
    • Jeschke, G.1
  • 7
    • 0036004918 scopus 로고    scopus 로고
    • Determination of the nanostructure of polymer materials by electron paramagnetic resonance spectroscopy
    • Jeschke G. Determination of the nanostructure of polymer materials by electron paramagnetic resonance spectroscopy. Macromol. Rapid Commun. 23 (2002) 227-246
    • (2002) Macromol. Rapid Commun. , vol.23 , pp. 227-246
    • Jeschke, G.1
  • 8
    • 3042819802 scopus 로고    scopus 로고
    • Data analysis procedures for pulse ELDOR measurements of broad distance distributions
    • Jeschke G., Panek G., Godt A., Bender A., and Paulsen H. Data analysis procedures for pulse ELDOR measurements of broad distance distributions. Appl. Magn. Reson. 26 (2004) 223-244
    • (2004) Appl. Magn. Reson. , vol.26 , pp. 223-244
    • Jeschke, G.1    Panek, G.2    Godt, A.3    Bender, A.4    Paulsen, H.5
  • 10
    • 0002767480 scopus 로고    scopus 로고
    • The primary and secondary accepters in bacterial photosynthesis III. Characterization of the quinone radicals QA(-)center dot and QB(-center dot) by EPR and ENDOR
    • Lubitz W., and Feher G. The primary and secondary accepters in bacterial photosynthesis III. Characterization of the quinone radicals QA(-)center dot and QB(-center dot) by EPR and ENDOR. Appl. Magn. Reson. 17 (1999) 1-48
    • (1999) Appl. Magn. Reson. , vol.17 , pp. 1-48
    • Lubitz, W.1    Feher, G.2
  • 11
    • 0001651984 scopus 로고    scopus 로고
    • Pulsed ENDOR at 95 GHz on the primary acceptor ubisemiquinone Q(A)(-center dot) in photosynthetic bacterial reaction centers and related model systems
    • Rohrer M., MacMillan F., Prisner T.F., Gardiner A.T., Möbius K., and Lubitz W. Pulsed ENDOR at 95 GHz on the primary acceptor ubisemiquinone Q(A)(-center dot) in photosynthetic bacterial reaction centers and related model systems. J. Phys. Chem. B 102 (1998) 4648-4657
    • (1998) J. Phys. Chem. B , vol.102 , pp. 4648-4657
    • Rohrer, M.1    MacMillan, F.2    Prisner, T.F.3    Gardiner, A.T.4    Möbius, K.5    Lubitz, W.6
  • 12
    • 0028063066 scopus 로고
    • Asymmetric binding of the primary acceptor quinone in reaction centers of the photosynthetic bacterium Rhodobacter sphaeroides R26, probed with Q-band (35 Ghz) Epr spectroscopy
    • van den Brink J.S., Spoyalov A.P., Gast P., van Liemt W.B.S., Raap J., Lugtenburg J., and Hoff A.J. Asymmetric binding of the primary acceptor quinone in reaction centers of the photosynthetic bacterium Rhodobacter sphaeroides R26, probed with Q-band (35 Ghz) Epr spectroscopy. FEBS Lett. 353 (1994) 273-276
    • (1994) FEBS Lett. , vol.353 , pp. 273-276
    • van den Brink, J.S.1    Spoyalov, A.P.2    Gast, P.3    van Liemt, W.B.S.4    Raap, J.5    Lugtenburg, J.6    Hoff, A.J.7
  • 13
    • 0037093869 scopus 로고    scopus 로고
    • Protein structure determination using long-distance constraints from double-quantum coherence ESR: study of T4 lysozyme
    • Borbat P.P., Mchaourab H.S., and Freed J.H. Protein structure determination using long-distance constraints from double-quantum coherence ESR: study of T4 lysozyme. J. Am. Chem. Soc. 124 (2002) 5304-5314
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5304-5314
    • Borbat, P.P.1    Mchaourab, H.S.2    Freed, J.H.3
  • 14
    • 0141681860 scopus 로고    scopus 로고
    • The origin of the spin density asymmetry at the Q(A) binding site of type II photosynthetic reaction centres
    • O'Malley P.J. The origin of the spin density asymmetry at the Q(A) binding site of type II photosynthetic reaction centres. Chem. Phys. Lett. 379 (2003) 277-281
    • (2003) Chem. Phys. Lett. , vol.379 , pp. 277-281
    • O'Malley, P.J.1
  • 15
    • 0022969389 scopus 로고
    • Primary photochemistry of iron-depleted and zinc-reconstituted reaction centers from rhodopseudomonas-sphaeroides
    • Kirmaier C., Holten D., Debus R.J., Feher G., and Okamura M.Y. Primary photochemistry of iron-depleted and zinc-reconstituted reaction centers from rhodopseudomonas-sphaeroides. Proc. Natl. Acad. Sci. USA 83 (1986) 6407-6411
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6407-6411
    • Kirmaier, C.1    Holten, D.2    Debus, R.J.3    Feher, G.4    Okamura, M.Y.5
  • 16
    • 0003086416 scopus 로고
    • Chemical composition and properties of reaction centers
    • Clayton R.K., and Sistrom W.R. (Eds), Plenum Press, New York
    • Feher G., and Okamura M.Y. Chemical composition and properties of reaction centers. In: Clayton R.K., and Sistrom W.R. (Eds). The Photosynthetic Bacteria (1978), Plenum Press, New York 349-386
    • (1978) The Photosynthetic Bacteria , pp. 349-386
    • Feher, G.1    Okamura, M.Y.2
  • 17
    • 0000231214 scopus 로고
    • Orientation of the primary quinone of bacterial photosynthetic reaction centers contained in chromatophore and reconstituted membranes/ion centers contained in chromatophore and reconstituted membranes
    • Tiede D.M., and Dutton P.L. Orientation of the primary quinone of bacterial photosynthetic reaction centers contained in chromatophore and reconstituted membranes/ion centers contained in chromatophore and reconstituted membranes. Biochim. Biophys. Acta 637 (1981) 278-290
    • (1981) Biochim. Biophys. Acta , vol.637 , pp. 278-290
    • Tiede, D.M.1    Dutton, P.L.2
  • 18
    • 33646384499 scopus 로고    scopus 로고
    • S. Stoll, PhD-thesis, ETH Zürich (2003).
  • 19
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • Stoll S., and Schweiger A. EasySpin, a comprehensive software package for spectral simulation and analysis in EPR. J. Magn. Reson. 178 (2006) 42-55
    • (2006) J. Magn. Reson. , vol.178 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 21
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • Pannier M., Veit S., Godt A., Jeschke G., and Spiess H.W. Dead-time free measurement of dipole-dipole interactions between electron spins. J. Magn. Reson. 142 (2000) 331-340
    • (2000) J. Magn. Reson. , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 22
    • 0029791152 scopus 로고    scopus 로고
    • Calculation of electron paramagnetic resonance spectra from Brownian dynamics trajectories: application to nitroxide side chains in proteins
    • Steinhoff H.J., and Hubbell W.L. Calculation of electron paramagnetic resonance spectra from Brownian dynamics trajectories: application to nitroxide side chains in proteins. Biophys. J. 71 (1996) 2201-2212
    • (1996) Biophys. J. , vol.71 , pp. 2201-2212
    • Steinhoff, H.J.1    Hubbell, W.L.2
  • 23
    • 0002121233 scopus 로고    scopus 로고
    • Molecular dynamics simulation and EPR spectroscopy of nitroxide side chains in bacteriorhodopsin
    • Steinhoff H.J., Müller M., Beier C., and Pfeiffer M. Molecular dynamics simulation and EPR spectroscopy of nitroxide side chains in bacteriorhodopsin. J. Mol. Liquids 84 (2000) 17-27
    • (2000) J. Mol. Liquids , vol.84 , pp. 17-27
    • Steinhoff, H.J.1    Müller, M.2    Beier, C.3    Pfeiffer, M.4
  • 24
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: a package for molecular simulation and trajectory analysis
    • Lindahl E., Hess B., and van der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7 (2001) 306-317
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 25
    • 33646380162 scopus 로고    scopus 로고
    • P. Gajula, I.V. Borovykh, C. Beier, P. Gast, T. Shkuropatova, H.-J. Steinhoff, Study of the structure and dynamics of spin-labeled photosynthetic reaction centers from Rhodobacter sphaeroides by electron paramagnetic resonance spectroscopy and molecular dynamics simulations, Appl. Magn. Reson. (submitted for publication).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.