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Volumn 1837, Issue 5, 2014, Pages 626-642

Channelrhodopsin unchained: Structure and mechanism of a light-gated cation channel

Author keywords

Bacteriorhodopsin; Electrophysiology; Optogenetics; Proton transfer; Vibrational spectroscopy

Indexed keywords

ASPARTIC ACID; BACTERIORHODOPSIN; CATION; CATION CHANNEL; CHANNELOPSIN; CHANNELRHODOPSIN; CHANNELRHODOPSIN 1; CHANNELRHODOPSIN 2; GLUTAMIC ACID; ION CHANNEL; PROTON; RHODOPSIN; SCHIFF BASE; UNCLASSIFIED DRUG;

EID: 84897113407     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2013.10.014     Document Type: Review
Times cited : (111)

References (179)
  • 1
    • 28544453561 scopus 로고    scopus 로고
    • Principles of selective ion transport in channels and pumps
    • DOI 10.1126/science.1113666
    • E. Gouaux, and R. Mackinnon Principles of selective ion transport in channels and pumps Science 310 2005 1461 1465 (Pubitemid 41746336)
    • (2005) Science , vol.310 , Issue.5753 , pp. 1461-1465
    • Gouaux, E.1    MacKinnon, R.2
  • 2
    • 10344233232 scopus 로고    scopus 로고
    • Ion homeostasis, channels, and transporters: An update on cellular mechanisms
    • G.R. Dubyak Ion homeostasis, channels, and transporters: an update on cellular mechanisms Adv. Physiol. Educ. 28 2004 143 154
    • (2004) Adv. Physiol. Educ. , vol.28 , pp. 143-154
    • Dubyak, G.R.1
  • 4
    • 31944452776 scopus 로고    scopus 로고
    • Mechanisms of valence selectivity in biological ion channels
    • DOI 10.1007/s00018-005-5405-8
    • B. Corry, and S.H. Chung Mechanisms of valence selectivity in biological ion channels Cell. Mol. Life Sci. 63 2006 301 315 (Pubitemid 43202312)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.3 , pp. 301-315
    • Corry, B.1    Chung, S.-H.2
  • 7
    • 0037189362 scopus 로고    scopus 로고
    • Channelrhodopsin-1: A light-gated proton channel in green algae
    • DOI 10.1126/science.1072068
    • G. Nagel, D. Ollig, M. Fuhrmann, S. Kateriya, A.M. Musti, E. Bamberg, and P. Hegemann Channelrhodopsin-1: a light-gated proton channel in green algae Science 296 2002 2395 2398 (Pubitemid 34734214)
    • (2002) Science , vol.296 , Issue.5577 , pp. 2395-2398
    • Nagel, G.1    Ollig, D.2    Fuhrmann, M.3    Kateriya, S.4    Musti, A.M.5    Bamberg, E.6    Hegemann, P.7
  • 9
    • 84855190225 scopus 로고    scopus 로고
    • New channelrhodopsin with a red-shifted spectrum and rapid kinetics from Mesostigma viride
    • e00115-11
    • E.G. Govorunova, E.N. Spudich, C.E. Lane, O.A. Sineshchekov, and J.L. Spudich New channelrhodopsin with a red-shifted spectrum and rapid kinetics from Mesostigma viride MBio 2 2011 e00115-11
    • (2011) MBio , vol.2
    • Govorunova, E.G.1    Spudich, E.N.2    Lane, C.E.3    Sineshchekov, O.A.4    Spudich, J.L.5
  • 10
    • 44349120639 scopus 로고    scopus 로고
    • Red-shifted optogenetic excitation: A tool for fast neural control derived from Volvox carteri
    • DOI 10.1038/nn.2120, PII NN2120
    • F. Zhang, M. Prigge, F. Beyrière, S.P. Tsunoda, J. Mattis, O. Yizhar, P. Hegemann, and K. Deisseroth Red-shifted optogenetic excitation: a tool for fast neural control derived from Volvox carteri Nat. Neurosci. 11 2008 631 633 (Pubitemid 351748117)
    • (2008) Nature Neuroscience , vol.11 , Issue.6 , pp. 631-633
    • Zhang, F.1    Prigge, M.2    Beyriere, F.3    Tsunoda, S.P.4    Mattis, J.5    Yizhar, O.6    Hegemann, P.7    Deisseroth, K.8
  • 13
    • 79959873914 scopus 로고    scopus 로고
    • The development and application of optogenetics
    • L. Fenno, O. Yizhar, and K. Deisseroth The development and application of optogenetics Annu. Rev. Neurosci. 34 2011 389 412
    • (2011) Annu. Rev. Neurosci. , vol.34 , pp. 389-412
    • Fenno, L.1    Yizhar, O.2    Deisseroth, K.3
  • 14
    • 44949122636 scopus 로고    scopus 로고
    • Algal sensory photoreceptors
    • DOI 10.1146/annurev.arplant.59.032607.092847
    • P. Hegemann Algal sensory photoreceptors Annu. Rev. Plant Biol. 59 2008 167 189 (Pubitemid 351813028)
    • (2008) Annual Review of Plant Biology , vol.59 , pp. 167-189
    • Hegemann, P.1
  • 15
    • 33749580770 scopus 로고    scopus 로고
    • The multitalented microbial sensory rhodopsins
    • DOI 10.1016/j.tim.2006.09.005, PII S0966842X06002319
    • J.L. Spudich The multitalented microbial sensory rhodopsins Trends Microbiol. 14 2006 480 487 (Pubitemid 44537810)
    • (2006) Trends in Microbiology , vol.14 , Issue.11 , pp. 480-487
    • Spudich, J.L.1
  • 17
    • 1942519407 scopus 로고    scopus 로고
    • Chlamydomonas Sensory Rhodopsins A and B: Cellular Content and Role in Photophobic Responses
    • E.G. Govorunova, K.H. Jung, O.A. Sineshchekov, and J.L. Spudich Chlamydomonas sensory rhodopsins A and B: cellular content and role in photophobic responses Biophys. J. 86 2004 2342 2349 (Pubitemid 38524422)
    • (2004) Biophysical Journal , vol.86 , Issue.4 , pp. 2342-2349
    • Govorunova, E.G.1    Jung, K.-H.2    Sineshchekov, O.A.3    Spudich, J.L.4
  • 18
    • 57349151754 scopus 로고    scopus 로고
    • Channelrhodopsin-1 initiates phototaxis and photophobic responses in Chlamydomonas by immediate light-induced depolarization
    • DOI 10.1105/tpc.108.057919
    • P. Berthold, S.P. Tsunoda, O.P. Ernst, W. Mages, D. Gradmann, and P. Hegemann Channelrhodopsin-1 initiates phototaxis and photophobic responses in Chlamydomonas by immediate light-induced depolarization Plant Cell 20 2008 1665 1677 (Pubitemid 352844170)
    • (2008) Plant Cell , vol.20 , Issue.6 , pp. 1665-1677
    • Berthold, P.1    Tsunoda, S.P.2    Ernst, O.P.3    Mages, W.4    Gradmann, D.5    Hegemanna, P.6
  • 19
    • 33749557420 scopus 로고    scopus 로고
    • Microbial rhodopsins: Functional versatility and genetic mobility
    • DOI 10.1016/j.tim.2006.09.006, PII S0966842X06002307
    • A.K. Sharma, J.L. Spudich, and W.F. Doolittle Microbial rhodopsins: functional versatility and genetic mobility Trends Microbiol. 14 2006 463 469 (Pubitemid 44537809)
    • (2006) Trends in Microbiology , vol.14 , Issue.11 , pp. 463-469
    • Sharma, A.K.1    Spudich, J.L.2    Doolittle, W.F.3
  • 21
    • 0030829631 scopus 로고    scopus 로고
    • Vision in microalgae
    • DOI 10.1007/s004250050191
    • P. Hegemann Vision in microalgae Planta 203 1997 265 274 (Pubitemid 27491020)
    • (1997) Planta , vol.203 , Issue.3 , pp. 265-274
    • Hegemann, P.1
  • 23
    • 78049261560 scopus 로고    scopus 로고
    • A user's guide to channelrhodopsin variants: Features, limitations and future developments
    • J.Y. Lin A user's guide to channelrhodopsin variants: features, limitations and future developments Exp. Physiol. 96 2010 19 25
    • (2010) Exp. Physiol. , vol.96 , pp. 19-25
    • Lin, J.Y.1
  • 25
    • 29044433616 scopus 로고    scopus 로고
    • Light activation of Channelrhodopsin-2 in excitable cells of caenorhabditis elegans triggers rapid behavioral responses
    • DOI 10.1016/j.cub.2005.11.032, PII S0960982205014077
    • G. Nagel, M. Brauner, J.F. Liewald, N. Adeishvili, E. Bamberg, and A. Gottschalk Light activation of channelrhodopsin-2 in excitable cells of Caenorhabditis elegans triggers rapid behavioral responses Curr. Biol. 15 2005 2279 2284 (Pubitemid 41790623)
    • (2005) Current Biology , vol.15 , Issue.24 , pp. 2279-2284
    • Nagel, G.1    Brauner, M.2    Liewald, J.F.3    Adeishvili, N.4    Bamberg, E.5    Gottschalk, A.6
  • 26
    • 37349092335 scopus 로고    scopus 로고
    • Spectral Characteristics of the Photocycle of Channelrhodopsin-2 and Its Implication for Channel Function
    • DOI 10.1016/j.jmb.2007.10.072, PII S0022283607014301
    • C. Bamann, T. Kirsch, G. Nagel, and E. Bamberg Spectral characteristics of the photocycle of channelrhodopsin-2 and its implication for channel function J. Mol. Biol. 375 2008 686 694 (Pubitemid 350297289)
    • (2008) Journal of Molecular Biology , vol.375 , Issue.3 , pp. 686-694
    • Bamann, C.1    Kirsch, T.2    Nagel, G.3    Bamberg, E.4
  • 27
    • 77749306541 scopus 로고    scopus 로고
    • Two open states with progressive proton selectivities in the branched channelrhodopsin-2 photocycle
    • A. Berndt, M. Prigge, D. Gradmann, and P. Hegemann Two open states with progressive proton selectivities in the branched channelrhodopsin-2 photocycle Biophys. J. 98 2010 753 761
    • (2010) Biophys. J. , vol.98 , pp. 753-761
    • Berndt, A.1    Prigge, M.2    Gradmann, D.3    Hegemann, P.4
  • 29
    • 65549100187 scopus 로고    scopus 로고
    • Characterization of engineered channelrhodopsin variants with improved properties and kinetics
    • J.Y. Lin, M.Z. Lin, P. Steinbach, and R.Y. Tsien Characterization of engineered channelrhodopsin variants with improved properties and kinetics Biophys. J. 96 2009 1803 1814
    • (2009) Biophys. J. , vol.96 , pp. 1803-1814
    • Lin, J.Y.1    Lin, M.Z.2    Steinbach, P.3    Tsien, R.Y.4
  • 30
    • 84879835185 scopus 로고    scopus 로고
    • Ion selectivity and competition in channelrhodopsins
    • F. Schneider, D. Gradmann, and P. Hegemann Ion selectivity and competition in channelrhodopsins Biophys. J. 105 2013 91 100
    • (2013) Biophys. J. , vol.105 , pp. 91-100
    • Schneider, F.1    Gradmann, D.2    Hegemann, P.3
  • 32
    • 84869784276 scopus 로고    scopus 로고
    • Re-introduction of transmembrane serine residues reduce the minimum pore diameter of channelrhodopsin-2
    • R. Richards, and R.E. Dempski Re-introduction of transmembrane serine residues reduce the minimum pore diameter of channelrhodopsin-2 PLoS One 7 2012 e50018
    • (2012) PLoS One , vol.7 , pp. 50018
    • Richards, R.1    Dempski, R.E.2
  • 33
    • 60849092562 scopus 로고    scopus 로고
    • Glu 87 of channelrhodopsin-1 causes pH-dependent color tuning and fast photocurrent inactivation
    • S.P. Tsunoda, and P. Hegemann Glu 87 of channelrhodopsin-1 causes pH-dependent color tuning and fast photocurrent inactivation Photochem. Photobiol. 85 2009 564 569
    • (2009) Photochem. Photobiol. , vol.85 , pp. 564-569
    • Tsunoda, S.P.1    Hegemann, P.2
  • 35
    • 53849119555 scopus 로고    scopus 로고
    • Ins and outs of major facilitator superfamily antiporters
    • C.J. Law, P.C. Maloney, and D.N. Wang Ins and outs of major facilitator superfamily antiporters Annu. Rev. Microbiol. 62 2008 289 305
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 289-305
    • Law, C.J.1    Maloney, P.C.2    Wang, D.N.3
  • 36
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • O. Jardetzky Simple allosteric model for membrane pumps Nature 211 1966 969 970
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 37
    • 80052461748 scopus 로고    scopus 로고
    • Rectification of the channelrhodopsin early conductance
    • D. Gradmann, A. Berndt, F. Schneider, and P. Hegemann Rectification of the channelrhodopsin early conductance Biophys. J. 101 2011 1057 1068
    • (2011) Biophys. J. , vol.101 , pp. 1057-1068
    • Gradmann, D.1    Berndt, A.2    Schneider, F.3    Hegemann, P.4
  • 38
    • 84877578341 scopus 로고    scopus 로고
    • Towards an understanding of channelrhodopsin function: Simulations lead to novel insights of the channel mechanism
    • H.C. Watanabe, K. Welke, D.J. Sindhikara, P. Hegemann, and M. Elstner Towards an understanding of channelrhodopsin function: simulations lead to novel insights of the channel mechanism J. Mol. Biol. 425 2013 1795 1814
    • (2013) J. Mol. Biol. , vol.425 , pp. 1795-1814
    • Watanabe, H.C.1    Welke, K.2    Sindhikara, D.J.3    Hegemann, P.4    Elstner, M.5
  • 39
    • 67349185408 scopus 로고    scopus 로고
    • Ion channels versus ion pumps: The principal difference, in principle
    • D.C. Gadsby Ion channels versus ion pumps: the principal difference, in principle Nat. Rev. Mol. Cell Biol. 10 2009 344 352
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 344-352
    • Gadsby, D.C.1
  • 40
    • 0022508431 scopus 로고
    • Anion transport systems in the plasma membrane of vertebrate cells
    • DOI 10.1016/0304-4157(86)90014-6
    • E.K. Hoffmann Anion transport systems in the plasma membrane of vertebrate cells Biochim. Biophys. Acta 864 1986 1 31 (Pubitemid 16083730)
    • (1986) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.864 , Issue.1 , pp. 1-31
    • Hoffmann, E.K.1
  • 41
    • 1542288949 scopus 로고    scopus 로고
    • - channels
    • DOI 10.1038/nature02314
    • - channels Nature 427 2004 803 807 (Pubitemid 38297735)
    • (2004) Nature , vol.427 , Issue.6977 , pp. 803-807
    • Accardi, A.1    Miller, C.2
  • 43
    • 33947305641 scopus 로고    scopus 로고
    • Transporters as channels
    • DOI 10.1146/annurev.physiol.69.031905.164816
    • L.J. DeFelice, and T. Goswami Transporters as channels Annu. Rev. Physiol. 69 2007 87 112 (Pubitemid 46457637)
    • (2007) Annual Review of Physiology , vol.69 , pp. 87-112
    • DeFelice, L.J.1    Goswami, T.2
  • 44
  • 46
    • 0001652299 scopus 로고
    • Time-course and stoichiometry of light-induced proton release and uptake during the photocycle of bacteriorhodopsin
    • S. Grzesiek, and N.A. Dencher Time-course and stoichiometry of light-induced proton release and uptake during the photocycle of bacteriorhodopsin FEBS Lett. 208 1986 337 342
    • (1986) FEBS Lett. , vol.208 , pp. 337-342
    • Grzesiek, S.1    Dencher, N.A.2
  • 53
    • 79960338849 scopus 로고    scopus 로고
    • Glutamate residue 90 in the predicted transmembrane domain 2 is crucial for cation flux through channelrhodopsin 2
    • K. Ruffert, B. Himmel, D. Lall, C. Bamann, E. Bamberg, H. Betz, and V. Eulenburg Glutamate residue 90 in the predicted transmembrane domain 2 is crucial for cation flux through channelrhodopsin 2 Biochem. Biophys. Res. Commun. 410 2011 737 743
    • (2011) Biochem. Biophys. Res. Commun. , vol.410 , pp. 737-743
    • Ruffert, K.1    Himmel, B.2    Lall, D.3    Bamann, C.4    Bamberg, E.5    Betz, H.6    Eulenburg, V.7
  • 55
    • 81055155876 scopus 로고    scopus 로고
    • Projection structure of channelrhodopsin-2 at 6 Å resolution by electron crystallography
    • M. Muller, C. Bamann, E. Bamberg, and W. Kuhlbrandt Projection structure of channelrhodopsin-2 at 6 Å resolution by electron crystallography J. Mol. Biol. 414 2011 86 95
    • (2011) J. Mol. Biol. , vol.414 , pp. 86-95
    • Muller, M.1    Bamann, C.2    Bamberg, E.3    Kuhlbrandt, W.4
  • 56
    • 0037093403 scopus 로고    scopus 로고
    • From structure to mechanism: Electron crystallographic studies of bacteriorhodopsin
    • S. Subramaniam, T. Hirai, and R. Henderson From structure to mechanism: electron crystallographic studies of bacteriorhodopsin Philos. Trans. R. Soc. Lond. A 360 2002 859 874
    • (2002) Philos. Trans. R. Soc. Lond. A , vol.360 , pp. 859-874
    • Subramaniam, S.1    Hirai, T.2    Henderson, R.3
  • 57
    • 77950283310 scopus 로고    scopus 로고
    • Studying the stoichiometries of membrane proteins by mass spectrometry: Microbial rhodopsins and a potassium ion channel
    • J. Hoffmann, L. Aslimovska, C. Bamann, C. Glaubitz, E. Bamberg, and B. Brutschy Studying the stoichiometries of membrane proteins by mass spectrometry: microbial rhodopsins and a potassium ion channel Phys. Chem. Chem. Phys. 12 2010 3480 3485
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 3480-3485
    • Hoffmann, J.1    Aslimovska, L.2    Bamann, C.3    Glaubitz, C.4    Bamberg, E.5    Brutschy, B.6
  • 59
    • 84884906995 scopus 로고    scopus 로고
    • Structural differences between the closed and open states of channelrhodopsin-2 as observed by EPR spectroscopy
    • N. Krause, C. Engelhard, J. Heberle, R. Schlesinger, and R. Bittl Structural differences between the closed and open states of channelrhodopsin-2 as observed by EPR spectroscopy FEBS Lett. 587 2013 3309 3313
    • (2013) FEBS Lett. , vol.587 , pp. 3309-3313
    • Krause, N.1    Engelhard, C.2    Heberle, J.3    Schlesinger, R.4    Bittl, R.5
  • 60
    • 58049216319 scopus 로고    scopus 로고
    • Monitoring light-induced structural changes of Channelrhodopsin-2 by UV-visible and Fourier transform infrared spectroscopy
    • E. Ritter, K. Stehfest, A. Berndt, P. Hegemann, and F.J. Bartl Monitoring light-induced structural changes of Channelrhodopsin-2 by UV-visible and Fourier transform infrared spectroscopy J. Biol. Chem. 283 2008 35033 35041
    • (2008) J. Biol. Chem. , vol.283 , pp. 35033-35041
    • Ritter, E.1    Stehfest, K.2    Berndt, A.3    Hegemann, P.4    Bartl, F.J.5
  • 62
    • 84872281071 scopus 로고    scopus 로고
    • Structural and spectral characterizations of C1C2 channelrhodopsin and its mutants by molecular simulations
    • M. Kamiya, H.E. Kato, R. Ishitani, O. Nureki, and S. Hayashi Structural and spectral characterizations of C1C2 channelrhodopsin and its mutants by molecular simulations Chem. Phys. Lett. 556 2013 266 271
    • (2013) Chem. Phys. Lett. , vol.556 , pp. 266-271
    • Kamiya, M.1    Kato, H.E.2    Ishitani, R.3    Nureki, O.4    Hayashi, S.5
  • 63
    • 33748903643 scopus 로고    scopus 로고
    • Proton transfers in the bacteriorhodopsin photocycle
    • DOI 10.1016/j.bbabio.2005.11.003, PII S0005272805002562
    • J.K. Lanyi Proton transfers in the bacteriorhodopsin photocycle Biochim. Biophys. Acta 1757 2006 1012 1018 (Pubitemid 44427748)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 1012-1018
    • Lanyi, J.K.1
  • 66
    • 75349085542 scopus 로고    scopus 로고
    • Structural guidance of the photocycle of channelrhodopsin-2 by an interhelical hydrogen bond
    • C. Bamann, R. Gueta, S. Kleinlogel, G. Nagel, and E. Bamberg Structural guidance of the photocycle of channelrhodopsin-2 by an interhelical hydrogen bond Biochemistry 49 2010 267 278
    • (2010) Biochemistry , vol.49 , pp. 267-278
    • Bamann, C.1    Gueta, R.2    Kleinlogel, S.3    Nagel, G.4    Bamberg, E.5
  • 69
    • 46249089993 scopus 로고    scopus 로고
    • Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins
    • DOI 10.1038/nature06977, PII NATURE06977
    • N.H. Joh, A. Min, S. Faham, J.P. Whitelegge, D. Yang, V.L. Woods, and J.U. Bowie Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins Nature 453 2008 1266 1270 (Pubitemid 351913594)
    • (2008) Nature , vol.453 , Issue.7199 , pp. 1266-1270
    • Joh, N.H.1    Min, A.2    Faham, S.3    Whitelegge, J.P.4    Yang, D.5    Woods Jr., V.L.6    Bowie, J.U.7
  • 71
    • 22144464025 scopus 로고    scopus 로고
    • A vibrational spectral maker for probing the hydrogen-bonding status of protonated Asp and Glu residues
    • DOI 10.1529/biophysj.104.047639
    • B. Nie, J. Stutzman, and A. Xie A vibrational spectral maker for probing the hydrogen-bonding status of protonated Asp and Glu residues Biophys. J. 88 2005 2833 2847 (Pubitemid 40976149)
    • (2005) Biophysical Journal , vol.88 , Issue.4 , pp. 2833-2847
    • Nie, B.1    Stutzman, J.2    Xie, A.3
  • 72
    • 49149092632 scopus 로고    scopus 로고
    • Correlation between the hydrogen-bond structures and the C = O stretching frequencies of carboxylic acids as studied by density functional theory calculations: Theoretical basis for interpretation of infrared bands of carboxylic groups in proteins
    • K. Takei, R. Takahashi, and T. Noguchi Correlation between the hydrogen-bond structures and the C = O stretching frequencies of carboxylic acids as studied by density functional theory calculations: theoretical basis for interpretation of infrared bands of carboxylic groups in proteins J. Phys. Chem. B 112 2008 6725 6731
    • (2008) J. Phys. Chem. B , vol.112 , pp. 6725-6731
    • Takei, K.1    Takahashi, R.2    Noguchi, T.3
  • 74
    • 0034055545 scopus 로고    scopus 로고
    • Structural changes in a cryo-cooled protein crystal owing to radiation damage
    • DOI 10.1107/S0907444999016261
    • W.P. Burmeister Structural changes in a cryo-cooled protein crystal owing to radiation damage Acta Crystallogr. D Biol. Crystallogr. 56 2000 328 341 (Pubitemid 30147184)
    • (2000) Acta Crystallographica Section D: Biological Crystallography , vol.56 , Issue.3 , pp. 328-341
    • Burmeister, W.P.1
  • 75
    • 16244392086 scopus 로고    scopus 로고
    • When X-rays modify the protein structure: Radiation damage at work
    • DOI 10.1016/j.tibs.2005.02.009
    • O. Carugo, and K. Djinovic Carugo When X-rays modify the protein structure: radiation damage at work Trends Biochem. Sci. 30 2005 213 219 (Pubitemid 40463311)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.4 , pp. 213-219
    • Carugo, O.1    Carugo, K.D.2
  • 76
    • 30744458117 scopus 로고    scopus 로고
    • Polarized FTIR spectroscopy in conjunction with in situ H/D exchange reveals the orientation of protein internal carboxylic acids
    • DOI 10.1021/ja056488r
    • F. Garczarek, and K. Gerwert Polarized FTIR spectroscopy in conjunction with in situ H/D exchange reveals the orientation of protein internal carboxylic acids J. Am. Chem. Soc. 128 2006 28 29 (Pubitemid 43100833)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.1 , pp. 28-29
    • Garczarek, F.1    Gerwert, K.2
  • 77
    • 84876717781 scopus 로고    scopus 로고
    • QM/MM simulations of vibrational spectra of bacteriorhodopsin and channelrhodopsin-2
    • K. Welke, H.C. Watanabe, T. Wolter, M. Gaus, and M. Elstner QM/MM simulations of vibrational spectra of bacteriorhodopsin and channelrhodopsin-2 Phys. Chem. Chem. Phys. 15 2013 6651 6659
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , pp. 6651-6659
    • Welke, K.1    Watanabe, H.C.2    Wolter, T.3    Gaus, M.4    Elstner, M.5
  • 78
    • 66249145702 scopus 로고    scopus 로고
    • Geometric characteristics of hydrogen bonds involving sulfur atoms in proteins
    • P. Zhou, F. Tian, F. Lv, and Z. Shang Geometric characteristics of hydrogen bonds involving sulfur atoms in proteins Proteins 76 2009 151 163
    • (2009) Proteins , vol.76 , pp. 151-163
    • Zhou, P.1    Tian, F.2    Lv, F.3    Shang, Z.4
  • 81
    • 20444370684 scopus 로고    scopus 로고
    • Functional characterization of sensory rhodopsin II from Halobacterium salinarum expressed in Escherichia coli
    • DOI 10.1016/j.febslet.2005.05.010, PII S0014579305005855
    • O.S. Mironova, R.G. Efremov, B. Person, J. Heberle, I.L. Budyak, G. Büldt, and R. Schlesinger Functional characterization of sensory rhodopsin II from Halobacterium salinarum expressed in Escherichia coli FEBS Lett. 579 2005 3147 3151 (Pubitemid 40797850)
    • (2005) FEBS Letters , vol.579 , Issue.14 , pp. 3147-3151
    • Mironova, O.S.1    Efremov, R.G.2    Person, B.3    Heberle, J.4    Budyak, I.L.5    Buldt, G.6    Schlesinger, R.7
  • 82
    • 71749109952 scopus 로고    scopus 로고
    • The retinal structure of channelrhodopsin-2 assessed by resonance Raman spectroscopy
    • M. Nack, I. Radu, C. Bamann, E. Bamberg, and J. Heberle The retinal structure of channelrhodopsin-2 assessed by resonance Raman spectroscopy FEBS Lett. 583 2009 3676 3680
    • (2009) FEBS Lett. , vol.583 , pp. 3676-3680
    • Nack, M.1    Radu, I.2    Bamann, C.3    Bamberg, E.4    Heberle, J.5
  • 83
    • 85005512115 scopus 로고
    • Application of Raman spectroscopy to retinal proteins Isr
    • T. Althaus, W. Eisfield, R. Lohrmann, and M. Stockburger Application of Raman spectroscopy to retinal proteins Isr J. Chem. 35 1995 227 251
    • (1995) J. Chem. , vol.35 , pp. 227-251
    • Althaus, T.1    Eisfield, W.2    Lohrmann, R.3    Stockburger, M.4
  • 84
    • 0025024705 scopus 로고
    • Color regulation in the archaebacterial phototaxis receptor phoborhodopsin (sensory rhodopsin II)
    • T. Takahashi, B. Yan, P. Mazur, F. Derguini, K. Nakanishi, and J.L. Spudich Color regulation in the archaebacterial phototaxis receptor phoborhodopsin (sensory rhodopsin II) Biochemistry 29 1990 8467 8474 (Pubitemid 20307828)
    • (1990) Biochemistry , vol.29 , Issue.36 , pp. 8467-8474
    • Takahashi, T.1    Yan, B.2    Mazur, P.3    Derguini, F.4    Nakanishi, K.5    Spudich, J.L.6
  • 85
    • 0017741644 scopus 로고
    • Resonance Raman studies of the purple membrane
    • DOI 10.1021/bi00632a029
    • B. Aton, A.G. Doukas, R.H. Callender, B. Becher, and T.G. Ebrey Resonance Raman studies of the purple membrane Biochemistry 16 1977 2995 2999 (Pubitemid 8185697)
    • (1977) Biochemistry , vol.16 , Issue.13 , pp. 2995-2999
    • Aton, B.1    Doukas, A.G.2    Callender, R.H.3
  • 86
    • 33646056953 scopus 로고    scopus 로고
    • Cytoplasmic shuttling of protons in Anabaena sensory rhodopsin: Implications for signaling mechanism
    • L. Shi, S.R. Yoon, A.G. Bezerra Jr., K.H. Jung, and L.S. Brown Cytoplasmic shuttling of protons in Anabaena sensory rhodopsin: implications for signaling mechanism J. Mol. Biol. 358 2006 686 700
    • (2006) J. Mol. Biol. , vol.358 , pp. 686-700
    • Shi, L.1    Yoon, S.R.2    Bezerra, Jr.A.G.3    Jung, K.H.4    Brown, L.S.5
  • 87
    • 0000942888 scopus 로고    scopus 로고
    • Fourier transform raman study of retinal isomeric composition and equilibration in halorhodopsin
    • L. Zimányi, and J.K. Lanyi Fourier transform Raman study of retinal isomeric composition and equilibration in halorhodopsin J. Phys. Chem. B 101 1997 1930 1933 (Pubitemid 127578359)
    • (1997) Journal of Physical Chemistry B , vol.101 , Issue.10 , pp. 1930-1933
    • Zimanyi, L.1    Lanyi, J.K.2
  • 88
    • 0021848415 scopus 로고
    • Determination of retinal chromophore structure in bacteriorhodopsin with resonance Raman spectroscopy
    • DOI 10.1007/BF01871263
    • S.O. Smith, J. Lugtenburg, and R.A. Mathies Determination of retinal chromophore structure in bacteriorhodopsin with resonance Raman spectroscopy J. Membr. Biol. 85 1985 95 109 (Pubitemid 15036784)
    • (1985) Journal of Membrane Biology , vol.85 , Issue.2 , pp. 95-109
    • Smith, S.O.1    Lugtenburg, J.2    Mathies, R.A.3
  • 89
    • 0000736928 scopus 로고
    • Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin
    • S.O. Smith, J.A. Pardoen, J. Lugtenburg, and R.A. Mathies Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin J. Am. Chem. Soc. 91 1987 804 819
    • (1987) J. Am. Chem. Soc. , vol.91 , pp. 804-819
    • Smith, S.O.1    Pardoen, J.A.2    Lugtenburg, J.3    Mathies, R.A.4
  • 90
    • 8844250818 scopus 로고    scopus 로고
    • Anabaena sensory rhodopsin: A photochromic color sensor at 2.0 A
    • DOI 10.1126/science.1103943
    • L. Vogeley, O.A. Sineshchekov, V.D. Trivedi, J. Sasaki, J.L. Spudich, and H. Luecke Anabaena sensory rhodopsin: a photochromic color sensor at 2.0 Å Science 306 2004 1390 1393 (Pubitemid 39532519)
    • (2004) Science , vol.306 , Issue.5700 , pp. 1390-1393
    • Vogeley, L.1    Sineshchekov, O.A.2    Trivedi, V.D.3    Sasaki, J.4    Spudich, J.L.5    Luecke, H.6
  • 92
    • 0000217440 scopus 로고
    • Role of water in bacteriorhodopsin's chromophore: Resonance Raman-study
    • P. Hildebrandt, and M. Stockburger Role of water in bacteriorhodopsin's chromophore: resonance Raman-study Biochemistry 23 1984 5539 5548
    • (1984) Biochemistry , vol.23 , pp. 5539-5548
    • Hildebrandt, P.1    Stockburger, M.2
  • 95
    • 44449102270 scopus 로고    scopus 로고
    • Microbial rhodopsins: Scaffolds for ion pumps, channels, and sensors
    • J.P. Klare, I. Chizhov, and M. Engelhard Microbial rhodopsins: scaffolds for ion pumps, channels, and sensors Results Probl. Cell Differ. 45 2008 73 122
    • (2008) Results Probl. Cell Differ. , vol.45 , pp. 73-122
    • Klare, J.P.1    Chizhov, I.2    Engelhard, M.3
  • 96
    • 85005688720 scopus 로고
    • The photocycles of bacteriorhodopsin
    • J.K. Lanyi, and G. Váró The photocycles of bacteriorhodopsin Isr. J. Chem. 35 1995 365 385
    • (1995) Isr. J. Chem. , vol.35 , pp. 365-385
    • Lanyi, J.K.1    Váró, G.2
  • 100
    • 77952304469 scopus 로고    scopus 로고
    • The branched photocycle of the slow-cycling channelrhodopsin-2 mutant C128T
    • K. Stehfest, E. Ritter, A. Berndt, F. Bartl, and P. Hegemann The branched photocycle of the slow-cycling channelrhodopsin-2 mutant C128T J. Mol. Biol. 398 2010 690 702
    • (2010) J. Mol. Biol. , vol.398 , pp. 690-702
    • Stehfest, K.1    Ritter, E.2    Berndt, A.3    Bartl, F.4    Hegemann, P.5
  • 101
    • 77951203251 scopus 로고    scopus 로고
    • Evolution of the channelrhodopsin photocycle model
    • K. Stehfest, and P. Hegemann Evolution of the channelrhodopsin photocycle model ChemPhysChem 11 2010 1120 1126
    • (2010) ChemPhysChem , vol.11 , pp. 1120-1126
    • Stehfest, K.1    Hegemann, P.2
  • 102
    • 78349292533 scopus 로고    scopus 로고
    • The photocycle of channelrhodopsin-2: Ultrafast reaction dynamics and subsequent reaction steps
    • M.K. Verhoefen, C. Bamann, R. Blocher, U. Förster, E. Bamberg, and J. Wachtveitl The photocycle of channelrhodopsin-2: ultrafast reaction dynamics and subsequent reaction steps ChemPhysChem 11 2010 3113 3122
    • (2010) ChemPhysChem , vol.11 , pp. 3113-3122
    • Verhoefen, M.K.1    Bamann, C.2    Blocher, R.3    Förster, U.4    Bamberg, E.5    Wachtveitl, J.6
  • 103
    • 84877250147 scopus 로고    scopus 로고
    • Ultrafast infrared spectroscopy on channelrhodopsin-2 reveals efficient energy transfer from the retinal chromophore to the protein
    • M.K. Neumann-Verhoefen, K. Neumann, C. Bamann, I. Radu, J. Heberle, E. Bamberg, and J.L. Wachtveitl Ultrafast infrared spectroscopy on channelrhodopsin-2 reveals efficient energy transfer from the retinal chromophore to the protein J. Am. Chem. Soc. 35 2013 6968 6976
    • (2013) J. Am. Chem. Soc. , vol.35 , pp. 6968-6976
    • Neumann-Verhoefen, M.K.1    Neumann, K.2    Bamann, C.3    Radu, I.4    Heberle, J.5    Bamberg, E.6    Wachtveitl, J.L.7
  • 104
    • 84861887132 scopus 로고    scopus 로고
    • Tuning the primary reaction of channelrhodopsin-2 by imidazole, pH, and site-specific mutations
    • F. Scholz, E. Bamberg, C. Bamann, and J. Wachtveitl Tuning the primary reaction of channelrhodopsin-2 by imidazole, pH, and site-specific mutations Biophys. J. 102 2012 2649 2657
    • (2012) Biophys. J. , vol.102 , pp. 2649-2657
    • Scholz, F.1    Bamberg, E.2    Bamann, C.3    Wachtveitl, J.4
  • 108
    • 85005616566 scopus 로고
    • Photoreactions of the Photointermediates of Bacteriorhodopsin
    • Photophysics and Photochemistry of Retinal Proteins
    • S.P. Balashov Photoreactions of the photointermediates of bacteriorhodopsin Isr. J. Chem. 35 1995 415 428 (Pubitemid 126081423)
    • (1995) Israel Journal of Chemistry , vol.35 , Issue.3-4 , pp. 415-428
    • Balashov, S.P.1
  • 109
    • 0027105851 scopus 로고
    • The back photoreaction of the M intermediate in the photocycle of bacteriorhodopsin: Mechanism and evidence for two M species
    • S. Druckmann, N. Friedman, J.K. Lanyi, R. Needleman, M. Ottolenghi, and M. Sheves The back photoreaction of the M intermediate in the photocycle of bacteriorhodopsin: mechanism and evidence for two M species Photochem. Photobiol. 56 1992 1041 1047
    • (1992) Photochem. Photobiol. , vol.56 , pp. 1041-1047
    • Druckmann, S.1    Friedman, N.2    Lanyi, J.K.3    Needleman, R.4    Ottolenghi, M.5    Sheves, M.6
  • 110
    • 82555168188 scopus 로고    scopus 로고
    • The chromophore structure of the long-lived intermediate of the C128T channelrhodopsin-2 variant
    • S. Bruun, H. Naumann, U. Kuhlmann, C. Schulz, K. Stehfest, P. Hegemann, and P. Hildebrandt The chromophore structure of the long-lived intermediate of the C128T channelrhodopsin-2 variant FEBS Lett. 585 2011 3998 4001
    • (2011) FEBS Lett. , vol.585 , pp. 3998-4001
    • Bruun, S.1    Naumann, H.2    Kuhlmann, U.3    Schulz, C.4    Stehfest, K.5    Hegemann, P.6    Hildebrandt, P.7
  • 111
    • 78650923932 scopus 로고    scopus 로고
    • Channelrhodopsin engineering and exploration of new optogenetic tools
    • P. Hegemann, and A. Moglich Channelrhodopsin engineering and exploration of new optogenetic tools Nat. Methods 8 2011 39 42
    • (2011) Nat. Methods , vol.8 , pp. 39-42
    • Hegemann, P.1    Moglich, A.2
  • 113
    • 0017334993 scopus 로고
    • Identification of retinal isomers isolated from bacteriorhodopsin
    • M.J. Pettei, A.P. Yudd, K. Nakanishi, R. Henselman, and W. Stoeckenius Identification of retinal isomers isolated from bacteriorhodopsin Biochemistry 16 1977 1955 1959 (Pubitemid 8088599)
    • (1977) Biochemistry , vol.16 , Issue.9 , pp. 1955-1959
    • Pettei, M.J.1    Yudd, A.P.2    Nakanishi, K.3
  • 114
    • 28444482132 scopus 로고    scopus 로고
    • Multiple photocycles of channelrhodopsin
    • DOI 10.1529/biophysj.105.069716
    • P. Hegemann, S. Ehlenbeck, and D. Gradmann Multiple photocycles of channelrhodopsin Biophys. J. 89 2005 3911 3918 (Pubitemid 41725613)
    • (2005) Biophysical Journal , vol.89 , Issue.6 , pp. 3911-3918
    • Hegemann, P.1    Ehlenbeck, S.2    Gradmann, D.3
  • 116
    • 84892900438 scopus 로고    scopus 로고
    • Computational modeling of channelrhodopsin-2 photocurrent characteristics in relation to neural signaling
    • R.A. Stefanescu, R.G. Shivakeshavan, P.P. Khargonekar, and S.S. Talathi Computational modeling of channelrhodopsin-2 photocurrent characteristics in relation to neural signaling Bull. Math. Biol. 75 2013 2208 2240
    • (2013) Bull. Math. Biol. , vol.75 , pp. 2208-2240
    • Stefanescu, R.A.1    Shivakeshavan, R.G.2    Khargonekar, P.P.3    Talathi, S.S.4
  • 117
    • 84876229081 scopus 로고    scopus 로고
    • Light-dark adaptation of Channelrhodopsin C128T mutant
    • E. Ritter, P. Piwowarski, P. Hegemann, and F.J. Bartl Light-dark adaptation of Channelrhodopsin C128T mutant J. Biol. Chem. 288 2013 10451 10458
    • (2013) J. Biol. Chem. , vol.288 , pp. 10451-10458
    • Ritter, E.1    Piwowarski, P.2    Hegemann, P.3    Bartl, F.J.4
  • 119
    • 0028136025 scopus 로고
    • Combined optical and photoelectric study of the photocycle of 13-cis bacteriorhodopsin
    • C. Gergely, C. Ganea, and G. Váró Combined optical and photoelectric study of the photocycle of 13-cis bacteriorhodopsin Biophys. J. 67 1994 855 861 (Pubitemid 24235414)
    • (1994) Biophysical Journal , vol.67 , Issue.2 , pp. 855-861
    • Gergely, C.1    Ganea, C.2    Varo, G.3
  • 120
    • 0024744044 scopus 로고
    • Photocycles of bacteriorhodopsin in light- and dark-adapted purple membrane studied by time-resolved absorption spectroscopy
    • J. Hofrichter, E.R. Henry, and R.H. Lozier Photocycles of bacteriorhodopsin in light- and dark-adapted purple membrane studied by time-resolved absorption spectroscopy Biophys. J. 56 1989 693 706
    • (1989) Biophys. J. , vol.56 , pp. 693-706
    • Hofrichter, J.1    Henry, E.R.2    Lozier, R.H.3
  • 121
    • 0028709095 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds
    • E. Goormaghtigh, V. Cabiaux, and J.M. Ruysschaert Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds Subcell. Biochem. 23 1994 329 362
    • (1994) Subcell. Biochem. , vol.23 , pp. 329-362
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 122
    • 85005500629 scopus 로고
    • Application of FTIR Spectroscopy to the Structural Study on the Function of Bacteriorhodopsin
    • Photophysics and Photochemistry of Retinal Proteins
    • A. Maeda Application of FTIR spectroscopy to the structural study on the function of bacteriorhodopsin Isr. J. Chem. 35 1995 387 400 (Pubitemid 126081421)
    • (1995) Israel Journal of Chemistry , vol.35 , Issue.3-4 , pp. 387-400
    • Maeda, A.1
  • 123
    • 0032476844 scopus 로고    scopus 로고
    • Determination of end-to-end distances in a series of TEMPO diradicals of up to 2.8 nm length with a new four-pulse double electron electron resonance experiment
    • R.E. Martin, M. Pannier, F. Diederich, V. Gramlich, M. Hubrich, and H.W. Spiess Determination of end-to-end distances in a series of TEMPO diradicals of up to 2.8 nm length with a new four-pulse double electron electron resonance experiment Angew. Chem. Int. Ed. 37 1998 2834 2837 (Pubitemid 29008565)
    • (1998) Angewandte Chemie - International Edition , vol.37 , Issue.20 , pp. 2834-2837
    • Martin, R.E.1    Pannier, M.2    Diederich, F.3    Gramlich, V.4    Hubrich, M.5    Spiess, H.W.6
  • 125
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • S. Krimm, and J. Bandekar Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins Adv. Protein Chem. 3 1986 181 364
    • (1986) Adv. Protein Chem. , vol.3 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 126
    • 0028709475 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures
    • E. Goormaghtigh, V. Cabiaux, and J.M. Ruysschaert Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures Subcell. Biochem. 23 1994 405 450
    • (1994) Subcell. Biochem. , vol.23 , pp. 405-450
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 127
    • 84875774981 scopus 로고    scopus 로고
    • Quantification of transition dipole strengths using 1D and 2D spectroscopy for the identification of molecular structures via exciton delocalization: Application to α-helices
    • M. Grechko, and M.T. Zanni Quantification of transition dipole strengths using 1D and 2D spectroscopy for the identification of molecular structures via exciton delocalization: application to α-helices J. Chem. Phys. 137 2012 184202
    • (2012) J. Chem. Phys. , vol.137 , pp. 184202
    • Grechko, M.1    Zanni, M.T.2
  • 128
    • 0000311181 scopus 로고
    • Evidence for light-induced 13-cis, 14-s-cis isomerization in bacteriorhodopsin obtained by FTIR difference spectroscopy using isotopically labelled retinals
    • K. Gerwert, and F. Siebert Evidence for light-induced 13-cis, 14-s-cis isomerization in bacteriorhodopsin obtained by FTIR difference spectroscopy using isotopically labelled retinals EMBO J. 5 1986 805 811
    • (1986) EMBO J. , vol.5 , pp. 805-811
    • Gerwert, K.1    Siebert, F.2
  • 129
    • 0035498355 scopus 로고    scopus 로고
    • Infrared methods for monitoring the protonation state of carboxylic amino acids in the photocycle of bacteriorhodopsin
    • DOI 10.1023/A:1013135419529
    • A.K. Dioumaev Infrared methods for monitoring the protonation state of carboxylic amino acids in the photocycle of bacteriorhodopsin Biochemistry (Mosc) 66 2001 1269 1276 (Pubitemid 34048184)
    • (2001) Biochemistry (Moscow) , vol.66 , Issue.11 , pp. 1269-1276
    • Dioumaev, A.K.1
  • 130
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • DOI 10.1016/S0079-6107(00)00021-3, PII S0079610700000213
    • A. Barth The infrared absorption of amino acid side chains Prog. Biophys. Mol. Biol. 74 2000 141 173 (Pubitemid 32168153)
    • (2000) Progress in Biophysics and Molecular Biology , vol.74 , Issue.3-5 , pp. 141-173
    • Barth, A.1
  • 131
    • 0024289369 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants: Light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
    • M.S. Braiman, T. Mogi, T. Marti, L.J. Stern, H.G. Khorana, and K.J. Rothschild Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212 Biochemistry 27 1988 8516 8520
    • (1988) Biochemistry , vol.27 , pp. 8516-8520
    • Braiman, M.S.1    Mogi, T.2    Marti, T.3    Stern, L.J.4    Khorana, H.G.5    Rothschild, K.J.6
  • 132
    • 0027249907 scopus 로고
    • Decoupling of photo- and proton cycle in the Asp85 → Glu mutant of bacteriorhodopsin
    • J. Heberle, D. Oesterhelt, and N.A. Dencher Decoupling of photo- and proton cycle in the Asp85 → Glu mutant of bacteriorhodopsin EMBO J. 12 1993 3721 3727 (Pubitemid 23282747)
    • (1993) EMBO Journal , vol.12 , Issue.10 , pp. 3721-3727
    • Heberle, J.1    Oesterhelt, D.2    Dencher, N.A.3
  • 133
    • 0025016817 scopus 로고
    • Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base
    • H. Otto, T. Marti, M. Holz, T. Mogi, L.J. Stern, F. Engel, H.G. Khorana, and M.P. Heyn Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base Proc. Natl. Acad. Sci. U. S. A. 87 1990 1018 1022
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 1018-1022
    • Otto, H.1    Marti, T.2    Holz, M.3    Mogi, T.4    Stern, L.J.5    Engel, F.6    Khorana, H.G.7    Heyn, M.P.8
  • 135
    • 0028015918 scopus 로고
    • Aspartic proteinases - Fourier transform IR studies of the aspartic carboxylic groups in the active site of pepsin
    • DOI 10.1016/0014-5793(94)00979-1
    • G. Iliadis, G. Zundel, and B. Brzezinski Aspartic proteinases - Fourier transform IR studies of the aspartic carboxylic groups in the active site of pepsin FEBS Lett. 352 1994 315 317 (Pubitemid 24302460)
    • (1994) FEBS Letters , vol.352 , Issue.3 , pp. 315-317
    • Zundel, G.1
  • 136
    • 0032562215 scopus 로고    scopus 로고
    • Existence of a proton transfer chain in bacteriorhodopsin: Participation of Glu-194 in the release of protons to the extracellular surface
    • DOI 10.1021/bi971842m
    • A.K. Dioumaev, H.T. Richter, L.S. Brown, M. Tanio, S. Tuzi, H. Saitô, Y. Kimura, R. Needleman, and J.K. Lanyi Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface Biochemistry 37 1998 2496 2506 (Pubitemid 28119325)
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2496-2506
    • Dioumaev, A.K.1    Richter, H.-T.2    Brown, L.S.3    Tanio, M.4    Tuzi, S.5    Saito, H.6    Kimura, Y.7    Needleman, R.8    Lanyi, J.K.9
  • 137
    • 77956589405 scopus 로고    scopus 로고
    • Directional proton transfer in membrane proteins achieved through protonated protein-bound water molecules: A proton diode
    • S. Wolf, E. Freier, M. Potschies, E. Hofmann, and K. Gerwert Directional proton transfer in membrane proteins achieved through protonated protein-bound water molecules: a proton diode Angew. Chem. Int. Ed. Engl. 49 2010 6889 6893
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 6889-6893
    • Wolf, S.1    Freier, E.2    Potschies, M.3    Hofmann, E.4    Gerwert, K.5
  • 138
    • 0028864699 scopus 로고
    • Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin
    • L.S. Brown, J. Sasaki, H. Kandori, A. Maeda, R. Needleman, and J.K. Lanyi Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin J. Biol. Chem. 270 1995 27122 27126
    • (1995) J. Biol. Chem. , vol.270 , pp. 27122-27126
    • Brown, L.S.1    Sasaki, J.2    Kandori, H.3    Maeda, A.4    Needleman, R.5    Lanyi, J.K.6
  • 139
    • 58149376459 scopus 로고    scopus 로고
    • Amino acids with an intermolecular proton bond as proton storage site in bacteriorhodopsin
    • P. Phatak, N. Ghosh, H. Yu, Q. Cui, and M. Elstner Amino acids with an intermolecular proton bond as proton storage site in bacteriorhodopsin Proc. Natl. Acad. Sci. U. S. A. 105 2008 19672 19677
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 19672-19677
    • Phatak, P.1    Ghosh, N.2    Yu, H.3    Cui, Q.4    Elstner, M.5
  • 140
    • 0033520062 scopus 로고    scopus 로고
    • Fourier transform infrared spectra of a late intermediate of the bacteriorhodopsin photocycle suggest transient protonation of Asp-212
    • A.K. Dioumaev, L.S. Brown, R. Needleman, and J.K. Lanyi Fourier transform infrared spectra of a late intermediate of the bacteriorhodopsin photocycle suggest transient protonation of Asp-212 Biochemistry 38 1999 10070 10078
    • (1999) Biochemistry , vol.38 , pp. 10070-10078
    • Dioumaev, A.K.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 141
    • 0031553201 scopus 로고    scopus 로고
    • Infrared difference spectra of the intermediates L, M, N, and O of the bacteriorhodopsin photoreaction obtained by time-resolved attenuated total reflection spectroscopy
    • C. Zscherp, and J. Heberle Infrared difference spectra of the intermediates L, M, N, and O of the bacteriorhodopsin photoreaction obtained by time-resolved attenuated total reflection spectroscopy J. Phys. Chem. B 101 1997 10542 10547 (Pubitemid 127587745)
    • (1997) Journal of Physical Chemistry B , vol.101 , Issue.49 , pp. 10542-10547
    • Zscherp, C.1    Heberle, J.2
  • 142
    • 0034789953 scopus 로고    scopus 로고
    • Time-resolved FT-IR spectroscopic investigation of the pH-dependent proton transfer reactions in the E194Q mutant of bacteriorhodopsin
    • DOI 10.1006/bbrc.2001.4730
    • C. Zscherp, R. Schlesinger, and J. Heberle Time-resolved FT-IR spectroscopic investigation of the pH-dependent proton transfer reactions in the E194Q mutant of bacteriorhodopsin Biochem. Biophys. Res. Commun. 283 2001 57 63 (Pubitemid 32912536)
    • (2001) Biochemical and Biophysical Research Communications , vol.283 , Issue.1 , pp. 57-63
    • Zscherp, C.1    Schlesinger, R.2    Heberle, J.3
  • 144
    • 0037197668 scopus 로고    scopus 로고
    • Proton transfers in the photochemical reaction cycle of proteorhodopsin
    • DOI 10.1021/bi025563x
    • A.K. Dioumaev, L.S. Brown, J. Shih, E.N. Spudich, J.L. Spudich, and J.K. Lanyi Proton transfers in the photochemical reaction cycle of proteorhodopsin Biochemistry 41 2002 5348 5358 (Pubitemid 34429369)
    • (2002) Biochemistry , vol.41 , Issue.17 , pp. 5348-5358
    • Dioumaev, A.K.1    Brown, L.S.2    Shih, J.3    Spudich, E.N.4    Spudich, J.L.5    Lanyi, J.K.6
  • 145
    • 62649112114 scopus 로고    scopus 로고
    • The photocycle and proton translocation pathway in a cyanobacterial ion-pumping rhodopsin
    • M.R. Miranda, A.R. Choi, L. Shi, A.G. Bezerra Jr., K.H. Jung, and L.S. Brown The photocycle and proton translocation pathway in a cyanobacterial ion-pumping rhodopsin Biophys. J. 96 2009 1471 1481
    • (2009) Biophys. J. , vol.96 , pp. 1471-1481
    • Miranda, M.R.1    Choi, A.R.2    Shi, L.3    Bezerra, Jr.A.G.4    Jung, K.H.5    Brown, L.S.6
  • 146
    • 0024325044 scopus 로고
    • A defective proton pump, point-mutated bacteriorhodopsin Asp96 → Asn is fully reactivated by azide
    • J. Tittor, C. Soell, D. Oesterhelt, H.J. Butt, and E. Bamberg A defective proton pump, point-mutated bacteriorhodopsin Asp96 → Asn is fully reactivated by azide EMBO J. 8 1989 3477 3482 (Pubitemid 19274392)
    • (1989) EMBO Journal , vol.8 , Issue.11 , pp. 3477-3482
    • Tittor, J.1    Soell, C.2    Oesterhelt, D.3    Butt, H.-J.4    Bamberg, E.5
  • 148
    • 34147114950 scopus 로고    scopus 로고
    • Inter-helical Hydrogen Bonds Are Essential Elements for Intra-protein Signal Transduction: The Role of Asp115 in Bacteriorhodopsin Transport Function
    • DOI 10.1016/j.jmb.2007.02.021, PII S0022283607002021
    • A. Perálvarez-Marín, V.A. Lórenz-Fonfría, J.-L. Bourdelande, E. Querol, H. Kandori, and E. Padrós Inter-helical hydrogen bonds are essential elements for intra-protein signal transduction: the role of Asp115 in bacteriorhodopsin transport function J. Mol. Biol. 368 2007 666 676 (Pubitemid 46553699)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.3 , pp. 666-676
    • Peralvarez-Marin, A.1    Lorenz-Fonfria, V.A.2    Bourdelande, J.-L.3    Querol, E.4    Kandori, H.5    Padros, E.6
  • 149
    • 33748793395 scopus 로고    scopus 로고
    • Influence of the membrane potential on the protonation of bacteriorhodopsin: Insights from electrostatic calculations into the regulation of proton pumping
    • DOI 10.1021/ja0619657
    • E. Bombarda, T. Becker, and G.M. Ullmann Influence of the membrane potential on the protonation of bacteriorhodopsin: insights from electrostatic calculations into the regulation of proton pumping J. Am. Chem. Soc. 128 2006 12129 12139 (Pubitemid 44413844)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.37 , pp. 12129-12139
    • Bombarda, E.1    Becker, T.2    Ullmann, G.M.3
  • 150
    • 0028067031 scopus 로고
    • Specific acceleration of de- and reprotonation steps by azide in mutated bacteriorhodopsins
    • DOI 10.1016/0005-2728(94)90109-0
    • J. Tittor, M. Wahl, U. Schweiger, and D. Oesterhelt Specific acceleration of deprotonation and reprotonation steps by azide in mutated bacteriorhodopsins Biochim. Biophys. Acta 1187 1994 191 197 (Pubitemid 24267053)
    • (1994) Biochimica et Biophysica Acta - Bioenergetics , vol.1187 , Issue.2 , pp. 191-197
    • Tittor, J.1    Wahl, M.2    Schweiger, U.3    Oesterhelt, D.4
  • 153
    • 0032492706 scopus 로고    scopus 로고
    • Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network
    • DOI 10.1021/bi971701k
    • R. Rammelsberg, G. Huhn, M. Lübben, and K. Gerwert Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network Biochemistry 37 1998 5001 5009 (Pubitemid 28175982)
    • (1998) Biochemistry , vol.37 , Issue.14 , pp. 5001-5009
    • Rammelsberg, R.1    Huhn, G.2    Lubben, M.3    Gerwert, K.4
  • 154
    • 0034734260 scopus 로고    scopus 로고
    • Protonation reactions and their coupling in bacteriorhodopsin
    • S.P. Balashov Protonation reactions and their coupling in bacteriorhodopsin Biochim. Biophys. Acta 1460 2000 75 94
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 75-94
    • Balashov, S.P.1
  • 156
    • 33748283409 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin following retinal photoisomerization from the 13-Cis form
    • DOI 10.1021/bi060958s
    • N. Mizuide, M. Shibata, N. Friedman, M. Sheves, M. Belenky, J. Herzfeld, and H. Kandori Structural changes in bacteriorhodopsin following retinal photoisomerization from the 13-cis form Biochemistry 45 2006 10674 10681 (Pubitemid 44320482)
    • (2006) Biochemistry , vol.45 , Issue.35 , pp. 10674-10681
    • Mizuide, N.1    Shibata, M.2    Friedman, N.3    Sheves, M.4    Belenky, M.5    Herzfeld, J.6    Kandori, H.7
  • 157
    • 33645661754 scopus 로고    scopus 로고
    • FTIR study of the photoisomerization processes in the 13-cis and all-trans forms of Anabaena sensory rhodopsin at 77 K
    • A. Kawanabe, Y. Furutani, K.H. Jung, and H. Kandori FTIR study of the photoisomerization processes in the 13-cis and all-trans forms of Anabaena sensory rhodopsin at 77 K Biochemistry 45 2006 4362 4370
    • (2006) Biochemistry , vol.45 , pp. 4362-4370
    • Kawanabe, A.1    Furutani, Y.2    Jung, K.H.3    Kandori, H.4
  • 158
    • 0024744044 scopus 로고
    • Photocycles of bacteriorhodopsin in light- and dark-adapted purple membrane studied by time-resolved absorption spectroscopy
    • J. Hofrichter, E.R. Henry, and R.H. Lozier Photocycles of bacteriorhodopsin in light- and dark-adapted purple membrane studied by time-resolved absorption spectroscopy Biophys. J. 56 1989 693 706
    • (1989) Biophys. J. , vol.56 , pp. 693-706
    • Hofrichter, J.1    Henry, E.R.2    Lozier, R.H.3
  • 159
    • 0027435427 scopus 로고
    • PH dependence of the formation of an M-type intermediate in the photocycle of 13-cis-bacteriorhodopsin
    • DOI 10.1016/0014-5793(93)80486-E
    • L.A. Drachev, S.V. Dracheva, and A.D. Kaulen pH dependence of the formation of an M-type intermediate in the photocycle of 13-cis- bacteriorhodopsin FEBS Lett. 332 1993 67 70 (Pubitemid 23295901)
    • (1993) FEBS Letters , vol.332 , Issue.1-2 , pp. 67-70
    • Drachev, L.A.1    Dracheva, S.V.2    Kaulen, A.D.3
  • 160
    • 0027946774 scopus 로고
    • Factors affecting the formation of an M-like intermediate in the photocycle of 13-cis-bacteriorhodopsin
    • DOI 10.1021/bi00207a010
    • G. Steinberg, M. Sheves, S. Bressler, and M. Ottolenghi Factors affecting the formation of an M-like intermediate in the photocycle of 13-cis-bacteriorhodopsin Biochemistry 33 1994 12439 12450 (Pubitemid 24340449)
    • (1994) Biochemistry , vol.33 , Issue.41 , pp. 12439-12450
    • Steinberg, G.1    Sheves, M.2    Bressler, S.3    Ottolenghi, M.4
  • 162
    • 0033005319 scopus 로고    scopus 로고
    • Bacterial rhodopsins: Evolution of a mechanistic model for the ion pumps
    • W. Stoeckenius Bacterial rhodopsins: evolution of a mechanistic model for the ion pumps Protein Sci. 8 1999 447 459 (Pubitemid 29072448)
    • (1999) Protein Science , vol.8 , Issue.2 , pp. 447-459
    • Stoeckenius, W.1
  • 163
    • 84897114580 scopus 로고    scopus 로고
    • Of ion pumps, sensors and channels - Perspectives on microbial rhodopsins between science and history
    • M. Grote, M. Engelhard, and P. Hegemann Of ion pumps, sensors and channels - perspectives on microbial rhodopsins between science and history Biochim. Biophys. Acta 1837 2013 533 545
    • (2013) Biochim. Biophys. Acta , vol.1837 , pp. 533-545
    • Grote, M.1    Engelhard, M.2    Hegemann, P.3
  • 166
    • 77955365677 scopus 로고    scopus 로고
    • Molecular impact of the membrane potential on the regulatory mechanism of proton transfer in sensory rhodopsin II
    • X. Jiang, M. Engelhard, K. Ataka, and J. Heberle Molecular impact of the membrane potential on the regulatory mechanism of proton transfer in sensory rhodopsin II J. Am. Chem. Soc. 132 2010 10808 10815
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 10808-10815
    • Jiang, X.1    Engelhard, M.2    Ataka, K.3    Heberle, J.4
  • 167
    • 0034805052 scopus 로고    scopus 로고
    • The voltage-dependent proton pumping in bacteriorhodopsin is characterized by optoelectric behavior
    • S. Geibel, T. Friedrich, P. Ormos, P.G. Wood, G. Nagel, and E. Bamberg The voltage-dependent proton pumping in bacteriorhodopsin is characterized by optoelectric behavior Biophys. J. 81 2001 2059 2068 (Pubitemid 32917156)
    • (2001) Biophysical Journal , vol.81 , Issue.4 , pp. 2059-2068
    • Geibel, S.1    Friedrich, T.2    Ormos, P.3    Wood, P.G.4    Nagel, G.5    Bamberg, E.6
  • 168
    • 0037763950 scopus 로고    scopus 로고
    • Electric-field dependent decays of two spectroscopically different M-states of photosensory rhodopsin II from Natronobacterium pharaonis
    • L. Rivas, S. Hippler-Mreyen, M. Engelhard, and P. Hildebrandt Electric-field dependent decays of two spectroscopically different M-states of photosensory rhodopsin II from Natronobacterium pharaonis Biophys. J. 84 2003 3864 3873 (Pubitemid 36637881)
    • (2003) Biophysical Journal , vol.84 , Issue.6 , pp. 3864-3873
    • Rivas, L.1    Hippler-Mreyen, S.2    Engelhard, M.3    Hildebrandt, P.4
  • 169
    • 84897115791 scopus 로고    scopus 로고
    • Hydrogen-bonding changes of internal water molecules upon the actions of microbial rhodopsins studied by FTIR spectroscopy
    • Y. Furutani, and H. Kandori Hydrogen-bonding changes of internal water molecules upon the actions of microbial rhodopsins studied by FTIR spectroscopy Biochim. Biophys. Acta 1837 2013 598 605
    • (2013) Biochim. Biophys. Acta , vol.1837 , pp. 598-605
    • Furutani, Y.1    Kandori, H.2
  • 170
    • 84897110085 scopus 로고    scopus 로고
    • The role of protein-bound water molecules in microbial rhodopsins
    • K. Gerwert, E. Freier, and S. Wolf The role of protein-bound water molecules in microbial rhodopsins Biochim. Biophys. Acta 1837 2013 606 613
    • (2013) Biochim. Biophys. Acta , vol.1837 , pp. 606-613
    • Gerwert, K.1    Freier, E.2    Wolf, S.3
  • 171
    • 33746795960 scopus 로고    scopus 로고
    • Time-resolved microspectroscopy on a single crystal of bacteriorhodopsin reveals lattice-induced differences in the photocycle kinetics
    • DOI 10.1529/biophysj.106.083345
    • R. Efremov, V.I. Gordeliy, J. Heberle, and G. Büldt Time-resolved microspectroscopy on a single crystal of bacteriorhodopsin reveals lattice-induced differences in the photocycle kinetics Biophys. J. 91 2006 1441 1451 (Pubitemid 44174261)
    • (2006) Biophysical Journal , vol.91 , Issue.4 , pp. 1441-1451
    • Efremov, R.1    Gordeliy, V.I.2    Heberle, J.3    Buldt, G.4
  • 173
    • 84897116696 scopus 로고    scopus 로고
    • Fluorescence spectroscopy of rhodopsins: Insights and approaches
    • U. Alexiev, and D.L. Farrens Fluorescence spectroscopy of rhodopsins: insights and approaches Biochim. Biophys. Acta 1837 2013 694 709
    • (2013) Biochim. Biophys. Acta , vol.1837 , pp. 694-709
    • Alexiev, U.1    Farrens, D.L.2
  • 175
    • 84867743209 scopus 로고    scopus 로고
    • Time-resolved structural studies at synchrotrons and X-ray free electron lasers: Opportunities and challenges
    • R. Neutze, and K. Moffat Time-resolved structural studies at synchrotrons and X-ray free electron lasers: opportunities and challenges Curr. Opin. Struct. Biol. 22 2012 651 659
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 651-659
    • Neutze, R.1    Moffat, K.2
  • 176
    • 70350593543 scopus 로고    scopus 로고
    • 4D nanoscale diffraction observed by convergent-beam ultrafast electron microscopy
    • A. Yurtsever, and A.H. Zewail 4D nanoscale diffraction observed by convergent-beam ultrafast electron microscopy Science 326 2009 708 712
    • (2009) Science , vol.326 , pp. 708-712
    • Yurtsever, A.1    Zewail, A.H.2
  • 177
    • 80052046145 scopus 로고    scopus 로고
    • Femtosecond electron diffraction: Heralding the era of atomically resolved dynamics
    • G. Sciaini, and R.J.D. Miller Femtosecond electron diffraction: heralding the era of atomically resolved dynamics Rep. Prog. Phys. 74 2011 096101
    • (2011) Rep. Prog. Phys. , vol.74 , pp. 096101
    • Sciaini, G.1    Miller, R.J.D.2
  • 178
    • 0034734254 scopus 로고    scopus 로고
    • Role of internal water molecules in bacteriorhodopsin
    • H. Kandori Role of internal water molecules in bacteriorhodopsin Biochim. Biophys. Acta 1460 2000 177 191
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 177-191
    • Kandori, H.1
  • 179
    • 77952572623 scopus 로고    scopus 로고
    • Protein fluctuations as the possible origin of the thermal activation of rod photoreceptors in the dark
    • V.A. Lórenz-Fonfría, Y. Furutani, T. Ota, K. Ido, and H. Kandori Protein fluctuations as the possible origin of the thermal activation of rod photoreceptors in the dark J. Am. Chem. Soc. 132 2010 5693 5703
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 5693-5703
    • Lórenz-Fonfría, V.A.1    Furutani, Y.2    Ota, T.3    Ido, K.4    Kandori, H.5


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