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Volumn 1, Issue 3, 2010, Pages 668-672

Drawing the retinal out of its comfort zone: An ONIOM(QM/MM) study of mutant squid rhodopsin

Author keywords

Biophysical chemistry

Indexed keywords

BIOPHYSICAL CHEMISTRY; COMFORT ZONE; COUNTERIONS; ELECTROSTATIC INTERACTIONS; SCHIFF-BASE; STRUCTURAL REARRANGEMENT; WATER MOLECULE;

EID: 77749267675     PISSN: None     EISSN: 19487185     Source Type: Journal    
DOI: 10.1021/jz100026k     Document Type: Article
Times cited : (16)

References (22)
  • 1
    • 43749109187 scopus 로고    scopus 로고
    • Crystal structure of squid rhodopsin
    • Murakami, M.; Kouyama, T. Crystal Structure of Squid Rhodopsin. Nature 2008, 453, 363-367.
    • (2008) Nature , vol.453 , pp. 363-367
    • Murakami, M.1    Kouyama, T.2
  • 4
    • 77749319224 scopus 로고    scopus 로고
    • Insights from structural and spectral tuning studies on squid rhodopsin
    • DOI: 10.1002/ chem.200903194
    • Insights from Structural and Spectral Tuning Studies on Squid Rhodopsin. Chem.;Eur. J. 2010, DOI: 10.1002/ chem.200903194.
    • (2010) Chem.;Eur. J.
  • 5
    • 0025653013 scopus 로고
    • Photophysics and molecular electronic applications of the rhodopsins
    • Birge, R. R. Photophysics and Molecular Electronic Applications of the Rhodopsins. Annu. Rev. Phys. Chem. 1990, 41, 683-733.
    • (1990) Annu. Rev. Phys. Chem. , vol.41 , pp. 683-733
    • Birge, R.R.1
  • 7
    • 0345713551 scopus 로고    scopus 로고
    • Hybrid models for combined quanum mechanical and molecular mechanical approaches
    • Bakowies, D.; Thiel,W. Hybrid Models for Combined Quanum Mechanical and Molecular Mechanical Approaches. J. Phys. Chem. 1996, 100, 10580-10594.
    • (1996) J. Phys. Chem. , vol.100 , pp. 10580-10594
    • Bakowies, D.1    Thiel, W.2
  • 8
    • 0344667545 scopus 로고    scopus 로고
    • A spectroscopy oriented configuration interaction procedure
    • Neese, F. A Spectroscopy Oriented Configuration Interaction Procedure. J. Chem. Phys. 2003, 119, 9428-9443.
    • (2003) J. Chem. Phys. , vol.119 , pp. 9428-9443
    • Neese, F.1
  • 9
    • 58149170421 scopus 로고    scopus 로고
    • Mechanismof spectral tuning going from retinal in vacuo to bovine rhodopsin and itsmutants: Multireference Ab initio and quantummechanics/ molecular mechanics studies
    • Altun, A.; Yokoyama, S.;Morokuma, K.Mechanismof Spectral Tuning Going from Retinal in Vacuo to Bovine Rhodopsin and itsMutants:Multireference Ab Initio and QuantumMechanics/ Molecular Mechanics Studies. J. Phys. Chem. B. 2008, 112, 16883-16890.
    • (2008) J. Phys. Chem. B. , vol.112 , pp. 16883-16890
    • Altun, A.1    Yokoyama, S.2    Morokuma, K.3
  • 10
    • 24944574732 scopus 로고    scopus 로고
    • Solvent and protein effects on the structure and dynamics of the rhodopsin chromophore.
    • Röhrig, U. F.; Guidoni, L.; Rothilsberger, U. Solvent and Protein Effects on the Structure and Dynamics of the Rhodopsin Chromophore. ChemPhysChem 2005, 6, 1836-1847.
    • (2005) ChemPhysChem , vol.6 , pp. 1836-1847
    • Röhrig, U.F.1    Guidoni, L.2    Rothilsberger, U.3
  • 11
    • 35848936525 scopus 로고    scopus 로고
    • An opsin shift in rhodopsin: Retinal s0-s1 excitation in protein, in solution and in the gas phase
    • Bravaya, K.; Bochenkova, A.; Granovsky, A.; Nemukhin, A. An Opsin Shift in Rhodopsin: Retinal S0-S1 Excitation in Protein, in Solution and in the Gas Phase. J. Am. Chem. Soc. 2007, 129, 13035-13042.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 13035-13042
    • Bravaya, K.1    Bochenkova, A.2    Granovsky, A.3    Nemukhin, A.4
  • 12
    • 0001612847 scopus 로고    scopus 로고
    • Femtosecond spectroscopy of 13-demethylrhodopsin visual pigment analogue: The role of nonbonded interactions in the isomerization process
    • Wang, Q.; Kochendoerfer, G. G.; Schoenlein, R.W.; Verdegem, P. J. E.; Lugtenburg, J.; Mathies, R. A.; Shank, C. V. Femtosecond Spectroscopy of 13-Demethylrhodopsin Visual Pigment Analogue: The Role of Nonbonded Interactions in the Isomerization Process. J. Phys. Chem. 1996, 100, 17388-17394.
    • (1996) J. Phys. Chem. , vol.100 , pp. 17388-17394
    • Wang, Q.1    Kochendoerfer, G.G.2    Schoenlein, R.W.3    Verdegem, P.J.E.4    Lugtenburg, J.5    Mathies, R.A.6    Shank, C.V.7
  • 13
    • 31144468743 scopus 로고    scopus 로고
    • Origin and consequences of steric strain in the rhodopsin binding pocket
    • Sugihara, M.; Hufen, J.; Buss, V. Origin and Consequences of Steric Strain in the Rhodopsin Binding Pocket. Biochemistry 2006, 45, 801-810.
    • (2006) Biochemistry , vol.45 , pp. 801-810
    • Sugihara, M.1    Hufen, J.2    Buss, V.3
  • 15
    • 0014194153 scopus 로고
    • Vision in octopus and squid
    • Hara, T.; Hara, R.; Takeuchi, J. Vision in Octopus and Squid. Nature 1967, 214, 572-573.
    • (1967) Nature , vol.214 , pp. 572-573
    • Hara, T.1    Hara, R.2    Takeuchi, J.3
  • 16
    • 33645527222 scopus 로고    scopus 로고
    • Computational studies of the primary phototransduction event in visual rhodopsin
    • Gascon, J. A.; Sproviero, E. M.; Batista, V. Computational Studies of the Primary Phototransduction Event in Visual Rhodopsin. Acc. Chem. Res. 2006, 39, 184-193.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 184-193
    • Gascon, J.A.1    Sproviero, E.M.2    Batista, V.3
  • 17
    • 33846807572 scopus 로고    scopus 로고
    • Protein assistance in the photoisomerization of rhodopsin and 9-cis-rhodopsin;insights fromexperiment and theory
    • Sekharan, S.; Sugihara, M.; Weingart, O.; Okada, T.; Buss, V. Protein Assistance in the Photoisomerization of Rhodopsin and 9-cis-Rhodopsin;Insights fromExperiment and Theory. J. Am. Chem. Soc. 2007, 129, 1052-1105
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 1052-1105
    • Sekharan, S.1    Sugihara, M.2    Weingart, O.3    Okada, T.4    Buss, V.5
  • 18
    • 34347212074 scopus 로고    scopus 로고
    • Coupled cluster studies of the lowest excited states of the 11-cis-retinal chromophore
    • Send, R.; Sundholm, D. Coupled Cluster Studies of the Lowest Excited States of the 11-cis-Retinal Chromophore. Phys. Chem. Chem. Phys. 2007, 9, 2862-2867.
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 2862-2867
    • Send, R.1    Sundholm, D.2
  • 19
    • 0005853391 scopus 로고
    • Two-photon spectroscopy of locked-11-cis-rhodopsin: Evidence for a protonated schiff base in the neutral protein binding site
    • Birge, R. R.; Murray, L. P.; Pierce, B. M.; Akita, H.; Balogh-Nair, V.; Findsen, L. A.; Nakanishi, K. Two-Photon Spectroscopy of Locked-11-cis- Rhodopsin: Evidence for a Protonated Schiff Base in the Neutral Protein Binding Site. Proc. Natl. Acad. Sci. U.S.A. 1985, 82, 4117-4121.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 4117-4121
    • Birge, R.R.1    Murray, L.P.2    Pierce, B.M.3    Akita, H.4    Balogh-Nair, V.5    Findsen, L.A.6    Nakanishi, K.7
  • 20
    • 0030174901 scopus 로고    scopus 로고
    • Fluorescent properties of protonated and unprotonated schiff bases of retinal at room temperature
    • Bachilo, S. M.; Bondarev, S. L.; Gillbro, T. Fluorescent Properties of Protonated and Unprotonated Schiff Bases of Retinal at Room Temperature. J. Photochem. Photobiol., B 1996, 34, 39-46.
    • (1996) J. Photochem. Photobiol., B , vol.34 , pp. 39-46
    • Bachilo, S.M.1    Bondarev, S.L.2    Gillbro, T.3
  • 21
    • 47249158505 scopus 로고    scopus 로고
    • The molecular structure of a curl-shaped retinal isomer
    • Send, R.; Sundholm, D. The Molecular Structure of a Curl-Shaped Retinal Isomer. J. Mol. Model. 2008, 14, 717-726.
    • (2008) J. Mol. Model. , vol.14 , pp. 717-726
    • Send, R.1    Sundholm, D.2
  • 22
    • 0018076990 scopus 로고
    • Circular dichroism of squid rhodopsin and its intermediates
    • Shichida, S.; Tokunaga, F.; Yoshizawa, T. Circular Dichroism of Squid Rhodopsin and its Intermediates. Biochim. Biophys. Acta 1978, 504, 413-430.
    • (1978) Biochim. Biophys. Acta , vol.504 , pp. 413-430
    • Shichida, S.1    Tokunaga, F.2    Yoshizawa, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.