메뉴 건너뛰기




Volumn 38, Issue 1, 2012, Pages 153-168

Conformational changes in the archaerhodopsin-3 proton pump: Detection of conserved strongly hydrogen bonded water networks

Author keywords

Archaerhodopsin 3; Bacteriorhodopsin; Biomembranes; Energy transduction; FTIR difference spectroscopy; Membrane protein; Protein conformational changes; Proton pump; Water networks

Indexed keywords

ARCHAERHODOPSIN 3; BACTERIAL PROTEIN; BACTERIORHODOPSIN; PROTON PUMP; SCHIFF BASE; UNCLASSIFIED DRUG; WATER;

EID: 84857649966     PISSN: 00920606     EISSN: 15730689     Source Type: Journal    
DOI: 10.1007/s10867-011-9246-4     Document Type: Article
Times cited : (15)

References (68)
  • 1
    • 0033534585 scopus 로고    scopus 로고
    • Evolution of the archaeal rhodopsins: Evolution rate changes by gene duplication and functional differentiation
    • DOI 10.1006/jmbi.1998.2286
    • K Ihara T Umemura I Katagiri T Kitajima-Ihara Y Sugiyama Y Kimura Y Mukohata 1999 Evolution of the archaeal rhodopsins: evolution rate changes by gene duplication and functional differentiation J. Mol. Biol. 285 163 174 10.1006/jmbi.1998.2286 (Pubitemid 29034034)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.1 , pp. 163-174
    • Ihara, K.1    Umemura, T.2    Katagiri, I.3    Kitajima-Ihara, T.4    Sugiyama, Y.5    Kimura, Y.6    Mukohata, Y.7
  • 2
    • 0016967752 scopus 로고
    • The purple membrane of salt-loving bacteria
    • 10.1038/scientificamerican0676-38
    • W Stoeckenius 1976 The purple membrane of salt-loving bacteria Sci. Am. 234 6 38 46 10.1038/scientificamerican0676-38
    • (1976) Sci. Am. , vol.234 , Issue.6 , pp. 38-46
    • Stoeckenius, W.1
  • 3
    • 2942556920 scopus 로고    scopus 로고
    • X-ray diffraction of bacteriorhodopsin photocycle intermediates
    • DOI 10.1080/09687680410001666345
    • JK Lanyi 2004 X-ray diffraction of bacteriorhodopsin photocycle intermediates Mol. Membr. Biol. 21 143 150 10.1080/09687680410001666345 (Pubitemid 38745643)
    • (2004) Molecular Membrane Biology , vol.21 , Issue.3 , pp. 143-150
    • Lanyi, J.K.1
  • 4
    • 0026643216 scopus 로고
    • Difference spectroscopy of bacteriorhodopsin: Toward a molecular model
    • 10.1007/BF00762674
    • KJ Rothschild FTIR 1992 difference spectroscopy of bacteriorhodopsin: toward a molecular model J. Bioenerg. Biomembr. 24 147 167 10.1007/BF00762674
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 147-167
    • Rothschild, K.J.1
  • 5
    • 2342460436 scopus 로고    scopus 로고
    • Bacteriorhodopsin
    • DOI 10.1146/annurev.physiol.66.032102.150049
    • JK Lanyi 2004 Bacteriorhodopsin Annu. Rev. Physiol. 66 665 688 10.1146/annurev.physiol.66.032102.150049 (Pubitemid 40614459)
    • (2004) Annual Review of Physiology , vol.66 , pp. 665-688
    • Lanyi, J.K.1
  • 6
    • 4944249406 scopus 로고    scopus 로고
    • 15N-labeled arginine
    • DOI 10.1021/bi049238g
    • Y Xiao MS Hutson M Belenky J Herzfeld MS Braiman 2004 Role of arginine-82 in fast proton release during the bacteriorhodopsin photocycle: a time-resolved FT-IR study of purple membranes containing 15N-labeled arginine Biochemistry 43 12809 12818 10.1021/bi049238g (Pubitemid 39331800)
    • (2004) Biochemistry , vol.43 , Issue.40 , pp. 12809-12818
    • Xiao, Y.1    Hutson, M.S.2    Belenky, M.3    Herzfeld, J.4    Braiman, M.S.5
  • 7
    • 0026602025 scopus 로고
    • Water structural changes in the bacteriorhodopsin photocycle: Analysis by Fourier-transform infrared spectroscopy
    • 10.1021/bi00117a023
    • A Maeda J Sasaki Y Shichida T Yoshizawa 1992 Water structural changes in the bacteriorhodopsin photocycle: analysis by Fourier-transform infrared spectroscopy J. Biochem. 31 462 467 10.1021/bi00117a023
    • (1992) J. Biochem. , vol.31 , pp. 462-467
    • Maeda, A.1    Sasaki, J.2    Shichida, Y.3    Yoshizawa, T.4
  • 8
    • 0042617088 scopus 로고
    • Water molecules are active during the primary photoreaction of bacteriorhodopsin
    • 1994SPIE.2089.118F 10.1117/12.166685
    • WB Fischer KJ Rothschild 1993 Water molecules are active during the primary photoreaction of bacteriorhodopsin Proc. SPIE 2089 118 1994SPIE.2089..118F 10.1117/12.166685
    • (1993) Proc. SPIE , vol.2089 , pp. 118
    • Fischer, W.B.1    Rothschild, K.J.2
  • 9
    • 0028073137 scopus 로고
    • Detection of a water molecule in the active-site of bacteriorhodopsin: Hydrogen bonding changes during the primary photoreaction
    • DOI 10.1021/bi00209a005
    • W Fischer S Sonar T Marti HG Khorana KJ Rothschild 1994 Detection of a water molecule in the active site of bacteriorhodopsin: hydrogen bonding changes during the primary photoreaction Biochemistry 33 12757 12762 10.1021/bi00209a005 (Pubitemid 24352864)
    • (1994) Biochemistry , vol.33 , Issue.43 , pp. 12757-12762
    • Fischer, W.B.1    Sonar, S.2    Marti, T.3    Khorana, H.G.4    Rothschild, K.J.5
  • 10
    • 79958192493 scopus 로고    scopus 로고
    • Vibrational spectroscopy of water in narrow nanopores
    • 10.1021/jp109037q
    • M Weinwurm C Dellago 2011 Vibrational spectroscopy of water in narrow nanopores J. Phys. Chem. B 115 5268 5277 10.1021/jp109037q
    • (2011) J. Phys. Chem. B , vol.115 , pp. 5268-5277
    • Weinwurm, M.1    Dellago, C.2
  • 12
    • 0001735391 scopus 로고
    • Hydrogen-bonded chains with large proton polarizability as charge conductors in proteins Bacteriorhodopsin and the F subunit of E. coli
    • 1994JMoSt.322.33Z 10.1016/0022-2860(94)87019-5
    • G Zundel 1994 Hydrogen-bonded chains with large proton polarizability as charge conductors in proteins Bacteriorhodopsin and the F subunit of E. coli. J. Mol. Struct. 322 33 42 1994JMoSt.322...33Z 10.1016/0022-2860(94)87019-5
    • (1994) J. Mol. Struct. , vol.322 , pp. 33-42
    • Zundel, G.1
  • 13
    • 33646058552 scopus 로고    scopus 로고
    • Crystal structures of archaerhodopsin-1 and -2: Common structural motif in archaeal light-driven proton pumps
    • 10.1016/j.jmb.2006.02.032
    • N Enami K Yoshimura M Murakami H Okumura K Ihara T Kouyama 2006 Crystal structures of archaerhodopsin-1 and -2: common structural motif in archaeal light-driven proton pumps J. Mol. Biol. 358 675 685 10.1016/j.jmb.2006.02.032
    • (2006) J. Mol. Biol. , vol.358 , pp. 675-685
    • Enami, N.1    Yoshimura, K.2    Murakami, M.3    Okumura, H.4    Ihara, K.5    Kouyama, T.6
  • 15
    • 84856454418 scopus 로고    scopus 로고
    • Optical recording of action potentials in mammalian neurons using a microbial rhodopsin
    • in press
    • Kralj, J.M., Douglass, A.D., Hochbaum, D.R., McLaurin, D., Cohen, A.E.: Optical recording of action potentials in mammalian neurons using a microbial rhodopsin. Nat. Methods (in press)
    • Nat. Methods
    • Kralj, J.M.1    Douglass, A.D.2    Hochbaum, D.R.3    McLaurin, D.4    Cohen, A.E.5
  • 16
    • 78650902662 scopus 로고    scopus 로고
    • Optogenetics
    • 10.1038/nmeth.f.324
    • K Deisseroth 2011 Optogenetics Nat. Methods 8 26 29 10.1038/nmeth.f.324
    • (2011) Nat. Methods , vol.8 , pp. 26-29
    • Deisseroth, K.1
  • 17
    • 79960979207 scopus 로고    scopus 로고
    • Proton transfer via a transient linear water-molecule chain in a membrane protein
    • 2011PNAS.10811435F 10.1073/pnas.1104735108
    • E Freier S Wolf K Gerwert 2011 Proton transfer via a transient linear water-molecule chain in a membrane protein Proc. Natl. Acad. Sci. U.S.A. 108 11435 11439 2011PNAS..10811435F 10.1073/pnas.1104735108
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 11435-11439
    • Freier, E.1    Wolf, S.2    Gerwert, K.3
  • 19
    • 30144445932 scopus 로고    scopus 로고
    • Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy
    • DOI 10.1038/nature04231
    • F Garczarek K Gerwert 2006 Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy Nature 439 109 112 2006Natur.439..109G 10.1038/nature04231 (Pubitemid 43053638)
    • (2006) Nature , vol.439 , Issue.7072 , pp. 109-112
    • Garczarek, F.1    Gerwert, K.2
  • 20
    • 0141592427 scopus 로고    scopus 로고
    • Conformational changes detected in a sensory rhodopsin II-transducer complex
    • DOI 10.1074/jbc.M303719200
    • V Bergo EN Spudich JL Spudich KJ Rothschild 2003 Conformational changes detected in a sensory rhodopsin II-transducer complex J. Biol. Chem. 278 36556 36562 10.1074/jbc.M303719200 (Pubitemid 37139986)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.38 , pp. 36556-36562
    • Bergo, V.1    Spudich, E.N.2    Spudich, J.L.3    Rothschild, K.J.4
  • 21
    • 3142779894 scopus 로고    scopus 로고
    • Structural changes in the photoactive site of proteorhodopsin during the primary photoreaction
    • DOI 10.1021/bi0361968
    • V Bergo JJ Amsden EN Spudich JL Spudich KJ Rothschild 2004 Structural changes in the photoactive site of proteorhodopsin during the primary photoreaction Biochemistry 43 9075 9083 10.1021/bi0361968 (Pubitemid 38924441)
    • (2004) Biochemistry , vol.43 , Issue.28 , pp. 9075-9083
    • Bergo, V.1    Amsden, J.J.2    Spudich, E.N.3    Spudich, J.L.4    Rothschild, K.J.5
  • 22
    • 40849100171 scopus 로고    scopus 로고
    • Protonation state of Glul42 differs in the green- and blue-absorbing variants of proteorhodopsin
    • DOI 10.1021/bi7018964
    • JM Kralj VB Bergo JJ Amsden EN Spudich JL Spudich KJ Rothschild 2008 Protonation state of Glu142 differs in the green- and blue-absorbing variants of proteorhodopsin Biochemistry 47 3447 3453 10.1021/bi7018964 (Pubitemid 351399233)
    • (2008) Biochemistry , vol.47 , Issue.11 , pp. 3447-3453
    • Kralj, J.M.1    Bergo, V.B.2    Amsden, J.J.3    Spudich, E.N.4    Spudich, J.L.5    Rothschild, K.J.6
  • 23
    • 34248193410 scopus 로고    scopus 로고
    • FTIR study of the retinal Schiff base and internal water molecules of proteorhodopsin
    • DOI 10.1021/bi700143g
    • D Ikeda Y Furutani H Kandori FTIR 2007 study of the retinal Schiff base and internal water molecules of proteorhodopsin Biochemistry 46 5365 5373 10.1021/bi700143g (Pubitemid 46717261)
    • (2007) Biochemistry , vol.46 , Issue.18 , pp. 5365-5373
    • Ikeda, D.1    Furutani, Y.2    Kandori, H.3
  • 24
    • 0020158459 scopus 로고
    • Infrared evidence that the Schiff base of bacteriorhodopsin is protonated: BR570 and K intermediates
    • 1982PNAS.79.4045R 10.1073/pnas.79.13.4045
    • K Rothschild H Marrero 1982 Infrared evidence that the Schiff base of bacteriorhodopsin is protonated: bR570 and K intermediates Proc. Natl. Acad. Sci. U.S.A. 79 4045 4049 1982PNAS...79.4045R 10.1073/pnas.79.13.4045
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 4045-4049
    • Rothschild, K.1    Marrero, H.2
  • 25
    • 0021103472 scopus 로고
    • Investigation of the primary photochemistry of bacteriorhodopsin by low-temperature Fourier-transform infrared spectroscopy
    • 10.1111/j.1432-1033.1983.tb07187.x
    • F Siebert W Maentele 1983 Investigation of the primary photochemistry of bacteriorhodopsin by low-temperature Fourier-transform infrared spectroscopy Eur. J. Biochem. 130 565 573 10.1111/j.1432-1033.1983.tb07187.x
    • (1983) Eur. J. Biochem. , vol.130 , pp. 565-573
    • Siebert, F.1    Maentele, W.2
  • 26
    • 0036727510 scopus 로고    scopus 로고
    • A Fourier-transform infrared study of Neurospora rhodopsin: Similarities with archaeal rhodopsins
    • 10.1562/0031-8655(20 02)076<0341:AFTI SO>2.0.CO;2
    • V Bergo EN Spudich JL Spudich KJ Rothschild 2002 A Fourier-transform infrared study of Neurospora rhodopsin: similarities with archaeal rhodopsins Photochem. Photobiol. 76 341 349 10.1562/0031-8655(2002)076<0341:AFTISO>2. 0.CO;2
    • (2002) Photochem. Photobiol. , vol.76 , pp. 341-349
    • Bergo, V.1    Spudich, E.N.2    Spudich, J.L.3    Rothschild, K.J.4
  • 27
    • 0035951066 scopus 로고    scopus 로고
    • Internal water molecules of pharaonis phoborhodopsin studied by low-temperature infrared spectroscopy
    • DOI 10.1021/bi011621n
    • H Kandori Y Furutani K Shimono Y Shichida N Kamo 2001 Internal water molecules of pharaonis phoborhodopsin studied by low-temperature infrared spectroscopy Biochemistry 40 15693 15698 10.1021/bi011621n (Pubitemid 34015197)
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15693-15698
    • Kandori, H.1    Furutani, Y.2    Shimono, K.3    Shichida, Y.4    Kamo, N.5
  • 28
    • 0023661084 scopus 로고
    • Tyrosine and carboxyl protonation changes in the bacteriorhodopsin photocycle. 2. Tyrosines-26 and -64
    • 10.1021/bi00395a021
    • P Roepe P Scherrer PL Ahl SK Das Gupta RA Bogomolni J Herzfeld KJ Rothschild 1987 Tyrosine and carboxyl protonation changes in the bacteriorhodopsin photocycle. 2. Tyrosines-26 and -64 Biochemistry 26 6708 6717 10.1021/bi00395a021
    • (1987) Biochemistry , vol.26 , pp. 6708-6717
    • Roepe, P.1    Scherrer, P.2    Ahl, P.L.3    Das Gupta, S.K.4    Bogomolni, R.A.5    Herzfeld, J.6    Rothschild, K.J.7
  • 29
    • 33744959429 scopus 로고    scopus 로고
    • Conformational changes in the photocycle of Anabaena sensory rhodopsin: Absence of the Schiff base counterion protonation signal
    • DOI 10.1074/jbc.M600033200
    • VB Bergo M Ntefidou VD Trivedi JJ Amsden JM Kralj KJ Rothschild JL Spudich 2006 Conformational changes in the photocycle of Anabaena sensory rhodopsin: absence of the Schiff base counterion protonation signal J. Biol. Chem. 281 15208 15214 10.1074/jbc.M600033200 (Pubitemid 43855110)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.22 , pp. 15208-15214
    • Bergo, V.B.1    Ntefidou, M.2    Trivedi, V.D.3    Amsden, J.J.4    Kralj, J.M.5    Rothschild, K.J.6    Spudich, J.L.7
  • 30
    • 55249102897 scopus 로고    scopus 로고
    • Different structural changes occur in blue- and green-proteorhodopsins during the primary photoreaction
    • 10.1021/bi800945t
    • JJ Amsden JM Kralj VB Bergo EN Spudich JL Spudich KJ Rothschild 2008 Different structural changes occur in blue- and green-proteorhodopsins during the primary photoreaction Biochemistry 47 11490 11498 10.1021/bi800945t
    • (2008) Biochemistry , vol.47 , pp. 11490-11498
    • Amsden, J.J.1    Kralj, J.M.2    Bergo, V.B.3    Spudich, E.N.4    Spudich, J.L.5    Rothschild, K.J.6
  • 31
    • 0020174654 scopus 로고
    • Fourier-transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts
    • 1982PNAS.79.4972B 10.1073/pnas.79.16.4972
    • K Bagley G Dollinger L Eisenstein AK Singh L Zimanyi 1982 Fourier-transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts Proc. Natl. Acad. Sci. U.S.A. 79 4972 4976 1982PNAS...79.4972B 10.1073/pnas.79.16.4972
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 4972-4976
    • Bagley, K.1    Dollinger, G.2    Eisenstein, L.3    Singh, A.K.4    Zimanyi, L.5
  • 32
    • 0021527915 scopus 로고
    • Primary photochemistry of bacteriorhodopsin: Comparison of Fourier-transform infrared difference spectra with resonance Raman spectra
    • 10.1111/j.1751-1097.1984.tb05359.x
    • KJ Rothschild H Marrero M Braiman R Mathies 1984 Primary photochemistry of bacteriorhodopsin: comparison of Fourier-transform infrared difference spectra with resonance Raman spectra Photochem. Photobiol. 40 675 679 10.1111/j.1751-1097.1984.tb05359.x
    • (1984) Photochem. Photobiol. , vol.40 , pp. 675-679
    • Rothschild, K.J.1    Marrero, H.2    Braiman, M.3    Mathies, R.4
  • 33
    • 0017741644 scopus 로고
    • Resonance Raman studies of the purple membrane
    • DOI 10.1021/bi00632a029
    • B Aton AG Doukas RH Callender B Becher TG Ebrey 1977 Resonance Raman studies of the purple membrane Biochemistry 16 2995 2999 10.1021/bi00632a029 (Pubitemid 8185697)
    • (1977) Biochemistry , vol.16 , Issue.13 , pp. 2995-2999
    • Aton, B.1    Doukas, A.G.2    Callender, R.H.3
  • 34
    • 0037304632 scopus 로고    scopus 로고
    • Methionine changes in bacteriorhodopsin detected by FTIR and cell-free selenomethionine substitution
    • V Bergo S Mamaev J Olejnik KJ Rothschild 2003 Methionine changes in bacteriorhodopsin detected by FTIR and cell-free selenomethionine substitution Biophys. J. 84 960 966 2003BpJ....84..960B 10.1016/S0006-3495(03)74912-1 (Pubitemid 36133421)
    • (2003) Biophysical Journal , vol.84 , Issue.2 , pp. 960-966
    • Bergo, V.1    Mamaev, S.2    Olejnik, J.3    Rothschild, K.J.4
  • 35
    • 0021887888 scopus 로고
    • Fourier transform infrared spectroscopic evidence for the existence of two conformations of the bacteriorhodopsin primary photoproduct at low temperature
    • DOI 10.1016/0005-2728(85)90036-2
    • KJ Rothschild P Roepe J Gillespie 1985 Fourier-transform infrared spectroscopic evidence for the existence of two conformations of the bacteriorhodopsin primary photoproduct at low temperature Biochim. Biophys. Acta. 808 140 148 10.1016/0005-2728(85)90036-2 (Pubitemid 15049512)
    • (1985) Biochimica et Biophysica Acta - Bioenergetics , vol.808 , Issue.1 , pp. 140-148
    • Rothschild, K.J.1    Roepe, P.2    Gillespie, J.3
  • 36
    • 34547471963 scopus 로고    scopus 로고
    • Bacteriorhodopsin photocycle at cryogenic temperatures reveals distributed barriers of conformational substates
    • DOI 10.1073/pnas.0703859104
    • AK Dioumaev JK Lanyi 2007 Bacteriorhodopsin photocycle at cryogenic temperatures reveals distributed barriers of conformational substates Proc. Natl. Acad. Sci. U.S.A. 104 9621 9626 2007PNAS..104.9621D 10.1073/pnas. 0703859104 (Pubitemid 47175316)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.23 , pp. 9621-9626
    • Dioumaev, A.K.1    Lanyi, J.K.2
  • 38
    • 0000736928 scopus 로고
    • Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin
    • 10.1021/j100288a011
    • SO Smith JA Pardoen J Lugtenburg RA Mathies 1987 Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin J. Phys. Chem. 91 804 819 10.1021/j100288a011
    • (1987) J. Phys. Chem. , vol.91 , pp. 804-819
    • Smith, S.O.1    Pardoen, J.A.2    Lugtenburg, J.3    Mathies, R.A.4
  • 39
    • 40849100171 scopus 로고    scopus 로고
    • Protonation state of Glul42 differs in the green- and blue-absorbing variants of proteorhodopsin
    • DOI 10.1021/bi7018964
    • JM Kralj VB Bergo JJ Amsden EN Spudich JL Spudich KJ Rothschild 2008 Protonation state of Glu142 differs in the green- and blue-absorbing variants of proteorhodopsin Biochemistry 47 3447 3453 10.1021/bi7018964 (Pubitemid 351399233)
    • (2008) Biochemistry , vol.47 , Issue.11 , pp. 3447-3453
    • Kralj, J.M.1    Bergo, V.B.2    Amsden, J.J.3    Spudich, E.N.4    Spudich, J.L.5    Rothschild, K.J.6
  • 40
    • 0037197668 scopus 로고    scopus 로고
    • Proton transfers in the photochemical reaction cycle of proteorhodopsin
    • DOI 10.1021/bi025563x
    • AK Dioumaev LS Brown J Shih EN Spudich JL Spudich JK Lanyi 2002 Proton transfers in the photochemical reaction cycle of proteorhodopsin Biochemistry 41 5348 5358 10.1021/bi025563x (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
  • 41
    • 0023676060 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants: I. Tyrosine-185 protonates and deprotonates during the photocycle
    • 10.1002/prot.340030403
    • MS Braiman T Mogi LJ Stern NR Hackett BH Chao HG Khorana KJ Rothschild 1988 Vibrational spectroscopy of bacteriorhodopsin mutants: I. Tyrosine-185 protonates and deprotonates during the photocycle Proteins 3 219 229 10.1002/prot.340030403
    • (1988) Proteins , vol.3 , pp. 219-229
    • Braiman, M.S.1    Mogi, T.2    Stern, L.J.3    Hackett, N.R.4    Chao, B.H.5    Khorana, H.G.6    Rothschild, K.J.7
  • 42
    • 0025764569 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants: Evidence that Asp-96 deprotonates during the M → N transition
    • O Bousché M Braiman YW He T Marti HG Khorana KJ Rothschild 1991 Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence that ASP-96 deprotonates during the M-N transition J. Biol. Chem. 266 11063 11067 (Pubitemid 21906912)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.17 , pp. 11063-11067
    • Bousche, O.1    Braiman, M.2    He, Y.-W.3    Marti, T.4    Khorana, H.G.5    Rothschild, K.J.6
  • 43
    • 0027031210 scopus 로고
    • Time-resolved Fourier-transform infrared spectroscopy of the bacteriorhodopsin mutant Tyr-185→Phe: Asp-96 reprotonates during O formation; Asp-85 and Asp-212 deprotonate during O decay
    • 10.1111/j.1751-1097.1992.tb09732.x
    • O Bousche S Sonar MP Krebs HG Khorana KJ Rothschild 1992 Time-resolved Fourier-transform infrared spectroscopy of the bacteriorhodopsin mutant Tyr-185→Phe: Asp-96 reprotonates during O formation; Asp-85 and Asp-212 deprotonate during O decay Photochem. Photobiol. 56 1085 1095 10.1111/j.1751-1097.1992.tb09732.x
    • (1992) Photochem. Photobiol. , vol.56 , pp. 1085-1095
    • Bousche, O.1    Sonar, S.2    Krebs, M.P.3    Khorana, H.G.4    Rothschild, K.J.5
  • 44
    • 0025968915 scopus 로고
    • Protein dynamics in the bacteriorhodopsin photocycle: Submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates
    • MS Braiman O Bousché KJ Rothschild 1991 Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier-transform infrared spectra of the L, M, and N photointermediates Proc. Natl. Acad. Sci. U.S.A. 88 2388 2392 1991PNAS...88.2388B 10.1073/pnas.88.6.2388 (Pubitemid 21916422)
    • (1991) Proceedings of the National Academy of Sciences of the United States of America , vol.88 , Issue.6 , pp. 2388-2392
    • Braiman, M.S.1    Bousche, O.2    Rothschild, K.J.3
  • 45
    • 0023661083 scopus 로고
    • Tyrosine and carboxyl protonation changes in the bacteriorhodopsin photocycle
    • 10.1021/bi00395a020
    • P Roepe PL Ahl SK Das Gupta J Herzfeld KJ Rothschild 1987 Tyrosine and carboxyl protonation changes in the bacteriorhodopsin photocycle Biochemistry 26 6696 6707 10.1021/bi00395a020
    • (1987) Biochemistry , vol.26 , pp. 6696-6707
    • Roepe, P.1    Ahl, P.L.2    Das Gupta, S.K.3    Herzfeld, J.4    Rothschild, K.J.5
  • 46
    • 0024289369 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants: Light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
    • 10.1021/bi00423a002
    • MS Braiman T Mogi T Marti LJ Stern HG Khorana KJ Rothschild 1988 Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212 Biochemistry 27 8516 8520 10.1021/bi00423a002
    • (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
  • 48
    • 0034734254 scopus 로고    scopus 로고
    • Role of internal water molecules in bacteriorhodopsin
    • 10.1016/S0005-2728(00)00138-9
    • H Kandori 2000 Role of internal water molecules in bacteriorhodopsin Biochim. Biophys. Acta 1460 177 191 10.1016/S0005-2728(00)00138-9
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 177-191
    • Kandori, H.1
  • 49
    • 0028073137 scopus 로고
    • Detection of a water molecule in the active-site of bacteriorhodopsin: Hydrogen bonding changes during the primary photoreaction
    • DOI 10.1021/bi00209a005
    • WB Fischer S Sonar T Marti HG Khorana KJ Rothschild 1994 Detection of a water molecule in the active-site of bacteriorhodopsin: hydrogen bonding changes during the primary photoreaction Biochemistry 33 12757 12762 10.1021/bi00209a005 (Pubitemid 24352864)
    • (1994) Biochemistry , vol.33 , Issue.43 , pp. 12757-12762
    • Fischer, W.B.1    Sonar, S.2    Marti, T.3    Khorana, H.G.4    Rothschild, K.J.5
  • 50
    • 0027065057 scopus 로고
    • 15N shift
    • DOI 10.1021/bi00165a001
    • A Maeda J Sasaki YJ Ohkita M Simpson J Herzfeld 1992 Tryptophan perturbation in the L intermediate of bacteriorhodopsin: Fourier transform infrared analysis with indole-15N shift Biochemistry 31 12543 12545 10.1021/bi00165a001 (Pubitemid 23016518)
    • (1992) Biochemistry , vol.31 , Issue.50 , pp. 12543-12545
    • Maeda, A.1    Sasaki, J.2    Ohkita, Y.J.3    Simpson, M.4    Herzfeld, J.5
  • 52
    • 33644986630 scopus 로고    scopus 로고
    • Structure and dynamics of OH-(aq)
    • 10.1021/ar040207n
    • ME Tuckerman A Chandra D Marx 2006 Structure and dynamics of OH-(aq) Acc. Chem. Res. 39 151 158 10.1021/ar040207n
    • (2006) Acc. Chem. Res. , vol.39 , pp. 151-158
    • Tuckerman, M.E.1    Chandra, A.2    Marx, D.3
  • 54
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the Photosynthetic Oxygen-Evolving Center
    • DOI 10.1126/science.1093087
    • KN Ferreira TM Iverson K Maghlaoui J Barber S Iwata 2004 Architecture of the photosynthetic oxygen-evolving center Science 303 1831 1838 2004Sci...303.1831F 10.1126/science.1093087 (Pubitemid 38374869)
    • (2004) Science , vol.303 , Issue.5665 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 55
    • 33645732495 scopus 로고    scopus 로고
    • Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase
    • 2006Natur.440.829B 10.1038/nature04619
    • I Belevich MI Verkhovsky M Wikstrom 2006 Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase Nature 440 829 832 2006Natur.440..829B 10.1038/nature04619
    • (2006) Nature , vol.440 , pp. 829-832
    • Belevich, I.1    Verkhovsky, M.I.2    Wikstrom, M.3
  • 57
    • 0034702762 scopus 로고    scopus 로고
    • Relocation of internal bound water in bacteriorhodopsin during the photoreaction of M at low temperatures: An FTIR study
    • DOI 10.1021/bi000190q
    • A Maeda FL Tomson RB Gennis H Kandori TG Ebrey SP Balashov 2000 Relocation of internal bound water in bacteriorhodopsin during the photoreaction of M at low temperatures: an FTIR study Biochemistry 39 10154 10162 10.1021/bi000190q (Pubitemid 30663037)
    • (2000) Biochemistry , vol.39 , Issue.33 , pp. 10154-10162
    • Maeda, A.1    Tomson, F.L.2    Gennis, R.B.3    Kandori, H.4    Ebrey, T.G.5    Balashov, S.P.6
  • 58
    • 0028279038 scopus 로고
    • Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: A Fourier-transform infrared spectroscopic study
    • A Maeda J Sasaki Y Yamazaki R Needleman JK Lanyi 1994 Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: a Fourier-transform infrared spectroscopic study Biochemistry 33 1713 1717 10.1021/bi00173a013 (Pubitemid 24089697)
    • (1994) Biochemistry , vol.33 , Issue.7 , pp. 1713-1717
    • Maeda, A.1    Sasaki, J.2    Yamazaki, Y.3    Needleman, R.4    Lanyi, J.K.5
  • 59
    • 0024289369 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants: Light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
    • 10.1021/bi00423a002
    • MS Braiman T Mogi T Marti LJ Stern HG Khorana KJ Rothschild 1988 Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212 Biochemistry 27 8516 8520 10.1021/bi00423a002
    • (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
  • 60
    • 0036968773 scopus 로고    scopus 로고
    • Crystallographic structure of the retinal and the protein after deprotonation of the schiff base: The switch in the bacteriorhodopsin photocycle
    • DOI 10.1016/S0022-2836(02)00682-4
    • J Lanyi B Schobert 2002 Crystallographic structure of the retinal and the protein after deprotonation of the Schiff base: the switch in the bacteriorhodopsin photocycle J. Mol. Biol. 321 727 737 10.1016/S0022-2836(02) 00682-4 (Pubitemid 36124807)
    • (2002) Journal of Molecular Biology , vol.321 , Issue.4 , pp. 727-737
    • Lanyi, J.K.1    Schobert, B.2
  • 61
    • 0028864699 scopus 로고
    • Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin
    • 10.1074/jbc.270.45.27122
    • LS Brown J Sasaki H Kandori A Maeda R Needleman JK Lanyi 1995 Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin J. Biol. Chem. 270 27122 27126 10.1074/jbc.270.45.27122
    • (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
  • 63
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution
    • DOI 10.1126/science.286.5438.255
    • H Luecke B Schobert HT Richter JP Cartailler JK Lanyi 1999 Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution Science 286 255 261 10.1126/science.286.5438.255 (Pubitemid 29484682)
    • (1999) Science , vol.286 , Issue.5438 , pp. 255-260
    • Luecke, H.1    Schobert, B.2    Richter, H.-T.3    Cartailler, J.-P.4    Lanyi, J.K.5
  • 64
    • 0038649076 scopus 로고    scopus 로고
    • Crystallographic structures of the M and N intermediates of bacteriorhodopsin: Assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base
    • DOI 10.1016/S0022-2836(03)00576-X
    • B Schobert LS Brown JK Lanyi 2003 Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base J. Mol. Biol. 330 553 570 10.1016/S0022-2836(03)00576-X (Pubitemid 36814053)
    • (2003) Journal of Molecular Biology , vol.330 , Issue.3 , pp. 553-570
    • Schobert, B.1    Brown, L.S.2    Lanyi, J.K.3
  • 65
    • 0037466289 scopus 로고    scopus 로고
    • 2′ intermediates of the photocycle
    • DOI 10.1016/S0022-2836(03)00263-8
    • JK Lanyi B Schobert 2003 Mechanism of proton transport in bacteriorhodopsin from crystallographic structures of the K, L, M1, M2, and M2' intermediates of the photocycle J. Mol. Biol. 328 439 450 10.1016/S0022-2836(03) 00263-8 (Pubitemid 36407586)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.2 , pp. 439-450
    • Lanyi, J.K.1    Schobert, B.2
  • 66
    • 18844385503 scopus 로고    scopus 로고
    • FTIR studies of internal water molecules in the Schiff base region of bacteriorhodopsin
    • DOI 10.1021/bi050122+
    • M Shibata H Kandori FTIR 2005 studies of internal water molecules in the Schiff base region of bacteriorhodopsin Biochemistry 44 7406 7413 10.1021/bi050122+ (Pubitemid 40695994)
    • (2005) Biochemistry , vol.44 , Issue.20 , pp. 7406-7413
    • Shibata, M.1    Kandori, H.2
  • 67
    • 58049187077 scopus 로고    scopus 로고
    • Spectral signatures of the pentagonal water cluster in bacteriorhodopsin
    • 10.1002/cphc.200800473
    • M Baer G Mathias IF Kuo DJ Tobias CJ Mundy D Marx 2008 Spectral signatures of the pentagonal water cluster in bacteriorhodopsin Chemphyschem. 9 2703 2707 10.1002/cphc.200800473
    • (2008) Chemphyschem. , vol.9 , pp. 2703-2707
    • Baer, M.1    Mathias, G.2    Kuo, I.F.3    Tobias, D.J.4    Mundy, C.J.5    Marx, D.6
  • 68
    • 0030840715 scopus 로고    scopus 로고
    • Localization and orientation of functional water molecules in bacteriorhodopsin as revealed by polarized Fourier transform infrared spectroscopy
    • M Hatanaka H Kandori A Maeda 1997 Localization and orientation of functional water molecules in bacteriorhodopsin as revealed by polarized Fourier-transform infrared spectroscopy Biophys. J. 73 1001 1006 10.1016/S0006-3495(97)78133-5 (Pubitemid 27337635)
    • (1997) Biophysical Journal , vol.73 , Issue.2 , pp. 1001-1006
    • Hatanaka, M.1    Kandori, H.2    Maeda, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.