메뉴 건너뛰기




Volumn 427, Issue 1, 2015, Pages 205-220

Directed evolution of gloeobacter violaceus rhodopsin spectral properties

Author keywords

fluorescent proteins; opsins; optogenetics; proton pumps; Retinal

Indexed keywords

BACTERIORHODOPSIN; CAROTENOID; GLOEOBACTER VIOLACEUS RHODOPSIN; PROTON PUMP; RETINAL; SALINIXANTHIN; SCHIFF BASE; UNCLASSIFIED DRUG; RHODOPSIN;

EID: 84919701343     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.06.015     Document Type: Article
Times cited : (75)

References (76)
  • 1
    • 0037031561 scopus 로고    scopus 로고
    • AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides
    • S. Masuda, and C.E. Bauer AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides Cell 110 2002 613 623
    • (2002) Cell , vol.110 , pp. 613-623
    • Masuda, S.1    Bauer, C.E.2
  • 2
    • 57349088665 scopus 로고    scopus 로고
    • Photoexcited CRY2 interacts with CIB1 to regulate transcription and floral initiation in Arabidopsis
    • H. Liu, X. Yu, K. Li, J. Klejnot, H. Yang, and D. Lisiero Photoexcited CRY2 interacts with CIB1 to regulate transcription and floral initiation in Arabidopsis Science 322 2008 1535 1539
    • (2008) Science , vol.322 , pp. 1535-1539
    • Liu, H.1    Yu, X.2    Li, K.3    Klejnot, J.4    Yang, H.5    Lisiero, D.6
  • 3
    • 78651396502 scopus 로고    scopus 로고
    • Light modulation of cellular cAMP by a small bacterial photoactivated adenylyl cyclase, bPAC, of the soil bacterium Beggiatoa
    • M. Stierl, P. Stumpf, D. Udwari, R. Gueta, R. Hagedorn, and A. Losi Light modulation of cellular cAMP by a small bacterial photoactivated adenylyl cyclase, bPAC, of the soil bacterium Beggiatoa J Biol Chem 286 2011 1181 1188
    • (2011) J Biol Chem , vol.286 , pp. 1181-1188
    • Stierl, M.1    Stumpf, P.2    Udwari, D.3    Gueta, R.4    Hagedorn, R.5    Losi, A.6
  • 4
    • 0037186598 scopus 로고    scopus 로고
    • A blue-light-activated adenylyl cyclase mediates photoavoidance in Euglena gracilis
    • M. Iseki, S. Matsunaga, A. Murakami, K. Ohno, K. Shiga, and K. Yoshida A blue-light-activated adenylyl cyclase mediates photoavoidance in Euglena gracilis Nature 415 2002 1047 1051
    • (2002) Nature , vol.415 , pp. 1047-1051
    • Iseki, M.1    Matsunaga, S.2    Murakami, A.3    Ohno, K.4    Shiga, K.5    Yoshida, K.6
  • 5
    • 78650647900 scopus 로고    scopus 로고
    • Natural and engineered photoactivated nucleotidyl cyclases for optogenetic applications
    • M.H. Ryu, O.V. Moskvin, J. Siltberg-Liberles, and M. Gomelsky Natural and engineered photoactivated nucleotidyl cyclases for optogenetic applications J Biol Chem 285 2010 41501 41508
    • (2010) J Biol Chem , vol.285 , pp. 41501-41508
    • Ryu, M.H.1    Moskvin, O.V.2    Siltberg-Liberles, J.3    Gomelsky, M.4
  • 6
    • 0016723355 scopus 로고
    • Bacteriorhodopsin: A light-driven proton pump in Halobacterium Halobium
    • R.H. Lozier, R.A. Bogomolni, and W. Stoeckenius Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium Biophys J 15 1975 955 962
    • (1975) Biophys J , vol.15 , pp. 955-962
    • Lozier, R.H.1    Bogomolni, R.A.2    Stoeckenius, W.3
  • 9
    • 57349151754 scopus 로고    scopus 로고
    • Channelrhodopsin-1 initiates phototaxis and photophobic responses in Chlamydomonas by immediate light-induced depolarization
    • 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
    • (2008) Plant Cell , vol.20 , pp. 1665-1677
    • Berthold, P.1    Tsunoda, S.P.2    Ernst, O.P.3    Mages, W.4    Gradmann, D.5    Hegemann, P.6
  • 10
    • 0037173051 scopus 로고    scopus 로고
    • Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamydomonas reinhardtii
    • O.A. Sineshchekov, K.H. Jung, and J.L. Spudich Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamydomonas reinhardtii Proc Natl Acad Sci USA 99 2002 8689 8694
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8689-8694
    • Sineshchekov, O.A.1    Jung, K.H.2    Spudich, J.L.3
  • 13
    • 77953479756 scopus 로고    scopus 로고
    • Potential of light-harvesting proton pumps for bioenergy applications
    • J.M. Walter, D. Greenfield, and J. Liphardt Potential of light-harvesting proton pumps for bioenergy applications Curr Opin Biotechnol 21 2010 265 270
    • (2010) Curr Opin Biotechnol , vol.21 , pp. 265-270
    • Walter, J.M.1    Greenfield, D.2    Liphardt, J.3
  • 14
    • 84878638156 scopus 로고    scopus 로고
    • Directed evolution of bacteriorhodopsin for applications in bioelectronics
    • N.L. Wagner, J.A. Greco, M.J. Ranaghan, and R.R. Birge Directed evolution of bacteriorhodopsin for applications in bioelectronics J R Soc Interface 10 2013 20130197
    • (2013) J R Soc Interface , vol.10 , pp. 20130197
    • Wagner, N.L.1    Greco, J.A.2    Ranaghan, M.J.3    Birge, R.R.4
  • 15
    • 78650865624 scopus 로고    scopus 로고
    • The promise of optogenetics in cell biology: Interrogating molecular circuits in space and time
    • J.E. Toettcher, C.A. Voigt, O.D. Weiner, and W.A. Lim The promise of optogenetics in cell biology: interrogating molecular circuits in space and time Nat Methods 8 2011 35 38
    • (2011) Nat Methods , vol.8 , pp. 35-38
    • Toettcher, J.E.1    Voigt, C.A.2    Weiner, O.D.3    Lim, W.A.4
  • 16
    • 79960497713 scopus 로고    scopus 로고
    • Electrical spiking in Escherichia coli probed with a fluorescent voltage-indicating protein
    • J.M. Kralj, D.R. Hochbaum, A.D. Douglass, and A.E. Cohen Electrical spiking in Escherichia coli probed with a fluorescent voltage-indicating protein Science 333 2011 345 348
    • (2011) Science , vol.333 , pp. 345-348
    • Kralj, J.M.1    Hochbaum, D.R.2    Douglass, A.D.3    Cohen, A.E.4
  • 17
    • 0034519206 scopus 로고    scopus 로고
    • Retinylidene proteins: Structures and functions from archaea to humans
    • J.L. Spudich, C.S. Yang, K.H. Jung, and E.N. Spudich Retinylidene proteins: structures and functions from archaea to humans Annu Rev Cell Dev Biol 16 2000 365 392
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 365-392
    • Spudich, J.L.1    Yang, C.S.2    Jung, K.H.3    Spudich, E.N.4
  • 19
    • 0025308868 scopus 로고
    • Effects of modified chromophores on the spectral sensitivity of salamander, squirrel and macaque cones
    • C.L. Makino, T.W. Kraft, R.A. Mathies, J. Lugtenburg, M.E. Miley, and R. van der Steen Effects of modified chromophores on the spectral sensitivity of salamander, squirrel and macaque cones J Physiol 424 1990 545 560
    • (1990) J Physiol , vol.424 , pp. 545-560
    • Makino, C.L.1    Kraft, T.W.2    Mathies, R.A.3    Lugtenburg, J.4    Miley, M.E.5    Van Der Steen, R.6
  • 21
    • 84885605921 scopus 로고    scopus 로고
    • Characterization of a highly efficient blue-shifted channelrhodopsin from the marine alga Platymonas subcordiformis
    • E.G. Govorunova, O.A. Sineshchekov, H. Li, R. Janz, and J.L. Spudich Characterization of a highly efficient blue-shifted channelrhodopsin from the marine alga Platymonas subcordiformis J Biol Chem 288 2013 29911 29922
    • (2013) J Biol Chem , vol.288 , pp. 29911-29922
    • Govorunova, E.G.1    Sineshchekov, O.A.2    Li, H.3    Janz, R.4    Spudich, J.L.5
  • 24
    • 0029922071 scopus 로고    scopus 로고
    • Spectral tuning and molecular evolution of rod visual pigments in the species flock of cottoid fish in Lake Baikal
    • D.M. Hunt, J. Fitzgibbon, S.J. Slobodyanyuk, and J.K. Bowmaker Spectral tuning and molecular evolution of rod visual pigments in the species flock of cottoid fish in Lake Baikal Vision Res 36 1996 1217 1224
    • (1996) Vision Res , vol.36 , pp. 1217-1224
    • Hunt, D.M.1    Fitzgibbon, J.2    Slobodyanyuk, S.J.3    Bowmaker, J.K.4
  • 25
    • 44649186755 scopus 로고    scopus 로고
    • Screening and characterization of proteorhodopsin color-tuning mutations in Escherichia coli with endogenous retinal synthesis
    • S.Y. Kim, S.A. Waschuk, L.S. Brown, and K.H. Jung Screening and characterization of proteorhodopsin color-tuning mutations in Escherichia coli with endogenous retinal synthesis Biochim Biophys Acta 1777 2008 504 513
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 504-513
    • Kim, S.Y.1    Waschuk, S.A.2    Brown, L.S.3    Jung, K.H.4
  • 26
    • 84880067062 scopus 로고    scopus 로고
    • A blue-shifted light-driven proton pump for neural silencing
    • Y. Sudo, A. Okazaki, H. Ono, J. Yagasaki, S. Sugo, and M. Kamiya A blue-shifted light-driven proton pump for neural silencing J Biol Chem 288 2013 20624 20632
    • (2013) J Biol Chem , vol.288 , pp. 20624-20632
    • Sudo, Y.1    Okazaki, A.2    Ono, H.3    Yagasaki, J.4    Sugo, S.5    Kamiya, M.6
  • 27
    • 79953185789 scopus 로고    scopus 로고
    • Spectral tuning in sensory rhodopsin i from Salinibacter ruber
    • Y. Sudo, Y. Yuasa, J. Shibata, D. Suzuki, and M. Homma Spectral tuning in sensory rhodopsin I from Salinibacter ruber J Biol Chem 286 2011 11328 11336
    • (2011) J Biol Chem , vol.286 , pp. 11328-11336
    • Sudo, Y.1    Yuasa, Y.2    Shibata, J.3    Suzuki, D.4    Homma, M.5
  • 28
    • 65549147690 scopus 로고    scopus 로고
    • Molecular determinants differentiating photocurrent properties of two channelrhodopsins from Chlamydomonas
    • H. Wang, Y. Sugiyama, T. Hikima, E. Sugano, H. Tomita, and T. Takahashi Molecular determinants differentiating photocurrent properties of two channelrhodopsins from Chlamydomonas J Biol Chem 284 2009 5685 5696
    • (2009) J Biol Chem , vol.284 , pp. 5685-5696
    • Wang, H.1    Sugiyama, Y.2    Hikima, T.3    Sugano, E.4    Tomita, H.5    Takahashi, T.6
  • 29
    • 84884906500 scopus 로고    scopus 로고
    • ReaChR: A red-shifted variant of channelrhodopsin enables deep transcranial optogenetic excitation
    • J.Y. Lin, P.M. Knutsen, A. Muller, D. Kleinfeld, and R.Y. Tsien ReaChR: a red-shifted variant of channelrhodopsin enables deep transcranial optogenetic excitation Nat Neurosci 16 2013 1499 1508
    • (2013) Nat Neurosci , vol.16 , pp. 1499-1508
    • Lin, J.Y.1    Knutsen, P.M.2    Muller, A.3    Kleinfeld, D.4    Tsien, R.Y.5
  • 31
    • 33745114416 scopus 로고    scopus 로고
    • Bacteriorhodopsin-like proteins of eubacteria and fungi: The extent of conservation of the haloarchaeal proton-pumping mechanism
    • L.S. Brown, and K.H. Jung Bacteriorhodopsin-like proteins of eubacteria and fungi: the extent of conservation of the haloarchaeal proton-pumping mechanism Photochem Photobiol Sci 5 2006 538 546
    • (2006) Photochem Photobiol Sci , vol.5 , pp. 538-546
    • Brown, L.S.1    Jung, K.H.2
  • 32
    • 35848936525 scopus 로고    scopus 로고
    • An opsin shift in rhodopsin: Retinal S0-S1 excitation in protein, in solution, and in the gas phase
    • K. Bravaya, A. Bochenkova, A. Granovsky, and A. Nemukhin An opsin shift in rhodopsin: retinal S0-S1 excitation in protein, in solution, and in the gas phase J Am Chem Soc 129 2007 13035 13042
    • (2007) J Am Chem Soc , vol.129 , pp. 13035-13042
    • Bravaya, K.1    Bochenkova, A.2    Granovsky, A.3    Nemukhin, A.4
  • 33
    • 63049084264 scopus 로고    scopus 로고
    • Model systems for understanding absorption tuning by opsin proteins
    • M.B. Nielsen Model systems for understanding absorption tuning by opsin proteins Chem Soc Rev 38 2009 913 924
    • (2009) Chem Soc Rev , vol.38 , pp. 913-924
    • Nielsen, M.B.1
  • 34
    • 85005558631 scopus 로고
    • Application of artificial pigments to structure determination and study of photoinduced transformations of retinal proteins
    • K. Nakanishi, and R. Crouch Application of artificial pigments to structure determination and study of photoinduced transformations of retinal proteins Isr J Chem 35 1995 253 272
    • (1995) Isr J Chem , vol.35 , pp. 253-272
    • Nakanishi, K.1    Crouch, R.2
  • 35
    • 0034818544 scopus 로고    scopus 로고
    • Study of the opsin shift of bacteriorhodopsin: Insight from QM/MM calculations with electronic polarization effects of the protein environment
    • H. Houjou, Y. Inoue, and M. Sakurai Study of the opsin shift of bacteriorhodopsin: insight from QM/MM calculations with electronic polarization effects of the protein environment J Phys Chem B 105 2001 867 879
    • (2001) J Phys Chem B , vol.105 , pp. 867-879
    • Houjou, H.1    Inoue, Y.2    Sakurai, M.3
  • 36
    • 84865483386 scopus 로고    scopus 로고
    • Quantum chemical modeling of rhodopsin mutants displaying switchable colors
    • F. Melaccio, N. Ferre, and M. Olivucci Quantum chemical modeling of rhodopsin mutants displaying switchable colors Phys Chem Chem Phys 14 2012 12485 12495
    • (2012) Phys Chem Chem Phys , vol.14 , pp. 12485-12495
    • Melaccio, F.1    Ferre, N.2    Olivucci, M.3
  • 37
    • 33751249931 scopus 로고    scopus 로고
    • The color of rhodopsins at the ab initio multiconfigurational perturbation theory resolution
    • P.B. Coto, A. Strambi, N. Ferre, and M. Olivucci The color of rhodopsins at the ab initio multiconfigurational perturbation theory resolution Proc Natl Acad Sci USA 103 2006 17154 17159
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17154-17159
    • Coto, P.B.1    Strambi, A.2    Ferre, N.3    Olivucci, M.4
  • 38
  • 39
    • 0344335730 scopus 로고
    • Aspartic acid-96 and aspartic acid-85 play a central role in the function of bacteriorhodopsin as a proton pump
    • H.J. Butt, K. Fendler, E. Bamberg, J. Tittor, and D. Oesterhelt Aspartic acid-96 and aspartic acid-85 play a central role in the function of bacteriorhodopsin as a proton pump EMBO J 8 1989 1657 1663
    • (1989) EMBO J , vol.8 , pp. 1657-1663
    • Butt, H.J.1    Fendler, K.2    Bamberg, E.3    Tittor, J.4    Oesterhelt, D.5
  • 40
    • 0038053899 scopus 로고    scopus 로고
    • Structural insights into the mechanism of proton pumping by bacteriorhodopsin
    • T. Hirai, and S. Subramaniam Structural insights into the mechanism of proton pumping by bacteriorhodopsin FEBS Lett 545 2003 2 8
    • (2003) FEBS Lett , vol.545 , pp. 2-8
    • Hirai, T.1    Subramaniam, S.2
  • 41
    • 0036203742 scopus 로고    scopus 로고
    • Investigations of ambient light emission at deep-sea hydrothermal vents
    • S.N. White, A.D. Chave, and G.T. Reynolds Investigations of ambient light emission at deep-sea hydrothermal vents J Geophys Res Solid Earth 107 2002 10.1029/2000JB000015
    • (2002) J Geophys Res Solid Earth , vol.107
    • White, S.N.1    Chave, A.D.2    Reynolds, G.T.3
  • 42
    • 0028988375 scopus 로고
    • Site-directed isotope labeling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: The peptide carbonyl group of Tyr 185 is structurally active during the bR → N transition
    • C.F. Ludlam, S. Sonar, C.P. Lee, M. Coleman, J. Herzfeld, and U.L. RajBhandary Site-directed isotope labeling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: the peptide carbonyl group of Tyr 185 is structurally active during the bR → N transition Biochemistry 34 1995 2 6
    • (1995) Biochemistry , vol.34 , pp. 2-6
    • Ludlam, C.F.1    Sonar, S.2    Lee, C.P.3    Coleman, M.4    Herzfeld, J.5    Rajbhandary, U.L.6
  • 43
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 Angstrom resolution
    • H. Luecke, B. Schobert, H.T. Richter, J.P. Cartailler, and J.K. Lanyi Structural changes in bacteriorhodopsin during ion transport at 2 Angstrom resolution Science 286 1999 255 260
    • (1999) Science , vol.286 , pp. 255-260
    • Luecke, H.1    Schobert, B.2    Richter, H.T.3    Cartailler, J.P.4    Lanyi, J.K.5
  • 44
    • 2442597248 scopus 로고    scopus 로고
    • The influence of a transmembrane pH gradient on protonation probabilities of bacteriorhodopsin: The structural basis of the back-pressure effect
    • N. Calimet, and G.M. Ullmann The influence of a transmembrane pH gradient on protonation probabilities of bacteriorhodopsin: the structural basis of the back-pressure effect J Mol Biol 339 2004 571 589
    • (2004) J Mol Biol , vol.339 , pp. 571-589
    • Calimet, N.1    Ullmann, G.M.2
  • 45
    • 72749109806 scopus 로고    scopus 로고
    • Reconstitution of Gloeobacter violaceus rhodopsin with a light-harvesting carotenoid antenna
    • E.S. Imasheva, S.P. Balashov, A.R. Choi, K.H. Jung, and J.K. Lanyi Reconstitution of Gloeobacter violaceus rhodopsin with a light-harvesting carotenoid antenna Biochemistry 48 2009 10948 10955
    • (2009) Biochemistry , vol.48 , pp. 10948-10955
    • Imasheva, E.S.1    Balashov, S.P.2    Choi, A.R.3    Jung, K.H.4    Lanyi, J.K.5
  • 47
    • 55949126022 scopus 로고    scopus 로고
    • Crystallographic structure of xanthorhodopsin, the light-driven proton pump with a dual chromophore
    • H. Luecke, B. Schobert, J. Stagno, E.S. Imasheva, J.M. Wang, and S.P. Balashov Crystallographic structure of xanthorhodopsin, the light-driven proton pump with a dual chromophore Proc Natl Acad Sci USA 105 2008 16561 16565
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 16561-16565
    • Luecke, H.1    Schobert, B.2    Stagno, J.3    Imasheva, E.S.4    Wang, J.M.5    Balashov, S.P.6
  • 48
    • 84856454418 scopus 로고    scopus 로고
    • Optical recording of action potentials in mammalian neurons using a microbial rhodopsin
    • J.M. Kralj, A.D. Douglass, D.R. Hochbaum, D. Maclaurin, and A.E. Cohen Optical recording of action potentials in mammalian neurons using a microbial rhodopsin Nat Methods 9 2012 90 95
    • (2012) Nat Methods , vol.9 , pp. 90-95
    • Kralj, J.M.1    Douglass, A.D.2    Hochbaum, D.R.3    Maclaurin, D.4    Cohen, A.E.5
  • 49
    • 0027333436 scopus 로고
    • The first step in vision occurs in femtoseconds: Complete blue and red spectral studies
    • L.A. Peteanu, R.W. Schoenlein, Q. Wang, R.A. Mathies, and C.V. Shank The first step in vision occurs in femtoseconds: complete blue and red spectral studies Proc Natl Acad Sci USA 90 1993 11762 11766
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11762-11766
    • Peteanu, L.A.1    Schoenlein, R.W.2    Wang, Q.3    Mathies, R.A.4    Shank, C.V.5
  • 50
    • 77957118887 scopus 로고    scopus 로고
    • Conical intersection dynamics of the primary photoisomerization event in vision
    • D. Polli, P. Altoe, O. Weingart, K.M. Spillane, C. Manzoni, and D. Brida Conical intersection dynamics of the primary photoisomerization event in vision Nature 467 2010 440 443
    • (2010) Nature , vol.467 , pp. 440-443
    • Polli, D.1    Altoe, P.2    Weingart, O.3    Spillane, K.M.4    Manzoni, C.5    Brida, D.6
  • 52
    • 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, and F. Engel 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 USA 87 1990 1018 1022
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1018-1022
    • Otto, H.1    Marti, T.2    Holz, M.3    Mogi, T.4    Stern, L.J.5    Engel, F.6
  • 53
    • 84856545301 scopus 로고    scopus 로고
    • Site-directed mutagenesis in bacteriorhodopsin mutants and their characterization for bioelectrical and biotechnological equipment
    • P. Saeedi, J.M. Moosaabadi, S.S. Sebtahmadi, M. Behmanesh, and J.F. Mehrabadi Site-directed mutagenesis in bacteriorhodopsin mutants and their characterization for bioelectrical and biotechnological equipment Biotechnol Lett 34 2012 455 462
    • (2012) Biotechnol Lett , vol.34 , pp. 455-462
    • Saeedi, P.1    Moosaabadi, J.M.2    Sebtahmadi, S.S.3    Behmanesh, M.4    Mehrabadi, J.F.5
  • 54
    • 85044694117 scopus 로고    scopus 로고
    • Generation and analysis of bacteriorhodopsin mutants with the potential for biotechnological applications
    • P. Saeedi, J.M. Moosaabadi, S.S. Sebtahmadi, J.F. Mehrabadi, M. Behmanesh, and H.R. Nejad Generation and analysis of bacteriorhodopsin mutants with the potential for biotechnological applications Bioengineered 3 2012 275 279
    • (2012) Bioengineered , vol.3 , pp. 275-279
    • Saeedi, P.1    Moosaabadi, J.M.2    Sebtahmadi, S.S.3    Mehrabadi, J.F.4    Behmanesh, M.5    Nejad, H.R.6
  • 55
    • 0031583474 scopus 로고    scopus 로고
    • Chloride and proton transport in bacteriorhodopsin mutant D85T: Different modes of ion translocation in a retinal protein
    • J. Tittor, U. Haupts, C. Haupts, D. Oesterhelt, A. Becker, and E. Bamberg Chloride and proton transport in bacteriorhodopsin mutant D85T: different modes of ion translocation in a retinal protein J Mol Biol 271 1997 405 416
    • (1997) J Mol Biol , vol.271 , pp. 405-416
    • Tittor, J.1    Haupts, U.2    Haupts, C.3    Oesterhelt, D.4    Becker, A.5    Bamberg, E.6
  • 56
    • 78649563681 scopus 로고    scopus 로고
    • Ultrafast photo-induced reaction dynamics in bacteriorhodopsin and its Trp mutants
    • J. Briand, J. Leonard, and S. Haacke Ultrafast photo-induced reaction dynamics in bacteriorhodopsin and its Trp mutants J Opt 12 2010 084004
    • (2010) J Opt , vol.12 , pp. 084004
    • Briand, J.1    Leonard, J.2    Haacke, S.3
  • 57
    • 0025873898 scopus 로고
    • Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation
    • T. Marti, H. Otto, T. Mogi, S.J. Rosselet, M.P. Heyn, and H.G. Khorana Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation J Biol Chem 266 1991 6919 6927
    • (1991) J Biol Chem , vol.266 , pp. 6919-6927
    • Marti, T.1    Otto, H.2    Mogi, T.3    Rosselet, S.J.4    Heyn, M.P.5    Khorana, H.G.6
  • 58
    • 0026564606 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants - Evidence that Thr-46 and Thr-89 form part of a transient network of hydrogen bonds
    • K.J. Rothschild, Y.W. He, S. Sonar, T. Marti, and H.G. Khorana Vibrational spectroscopy of bacteriorhodopsin mutants - evidence that Thr-46 and Thr-89 form part of a transient network of hydrogen bonds J Biol Chem 267 1992 1615 1622
    • (1992) J Biol Chem , vol.267 , pp. 1615-1622
    • Rothschild, K.J.1    He, Y.W.2    Sonar, S.3    Marti, T.4    Khorana, H.G.5
  • 59
    • 0030913277 scopus 로고    scopus 로고
    • Threonine-89 participates in the active site of bacteriorhodopsin: Evidence for a role in color regulation and Schiff base proton transfer
    • T.S. Russell, M. Coleman, P. Rath, A. Nilsson, and K.J. Rothschild Threonine-89 participates in the active site of bacteriorhodopsin: evidence for a role in color regulation and Schiff base proton transfer Biochemistry-US 36 1997 7490 7497
    • (1997) Biochemistry-US , vol.36 , pp. 7490-7497
    • Russell, T.S.1    Coleman, M.2    Rath, P.3    Nilsson, A.4    Rothschild, K.J.5
  • 60
    • 0024978461 scopus 로고
    • Structure-function studies on bacteriorhodopsin. IX. Substitutions of tryptophan residues affect protein-retinal interactions in bacteriorhodopsin
    • T. Mogi, T. Marti, and H.G. Khorana Structure-function studies on bacteriorhodopsin. IX. Substitutions of tryptophan residues affect protein-retinal interactions in bacteriorhodopsin J Biol Chem 264 1989 14197 14201
    • (1989) J Biol Chem , vol.264 , pp. 14197-14201
    • Mogi, T.1    Marti, T.2    Khorana, H.G.3
  • 62
    • 0025991585 scopus 로고
    • Replacement of leucine-93 by alanine or threonine slows down the decay of the N and O intermediates in the photocycle of bacteriorhodopsin: Implications for proton uptake and 13-cis-retinal-all-trans-retinal reisomerization
    • S. Subramaniam, D.A. Greenhalgh, P. Rath, K.J. Rothschild, and H.G. Khorana Replacement of leucine-93 by alanine or threonine slows down the decay of the N and O intermediates in the photocycle of bacteriorhodopsin: implications for proton uptake and 13-cis-retinal-all-trans-retinal reisomerization Proc Natl Acad Sci USA 88 1991 6873 6877
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6873-6877
    • Subramaniam, S.1    Greenhalgh, D.A.2    Rath, P.3    Rothschild, K.J.4    Khorana, H.G.5
  • 63
    • 0027218962 scopus 로고
    • Hydrophobic amino acids in the retinal-binding pocket of bacteriorhodopsin
    • D.A. Greenhalgh, D.L. Farrens, S. Subramaniam, and H.G. Khorana Hydrophobic amino acids in the retinal-binding pocket of bacteriorhodopsin J Biol Chem 268 1993 20305 20311
    • (1993) J Biol Chem , vol.268 , pp. 20305-20311
    • Greenhalgh, D.A.1    Farrens, D.L.2    Subramaniam, S.3    Khorana, H.G.4
  • 64
    • 0025325371 scopus 로고
    • Effect of genetic modification of tyrosine-185 on the proton pump and the blue-to-purple transition in bacteriorhodopsin
    • D.J. Jang, M.A. el-Sayed, L.J. Stern, T. Mogi, and H.G. Khorana Effect of genetic modification of tyrosine-185 on the proton pump and the blue-to-purple transition in bacteriorhodopsin Proc Natl Acad Sci USA 87 1990 4103 4107
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4103-4107
    • Jang, D.J.1    El-Sayed, M.A.2    Stern, L.J.3    Mogi, T.4    Khorana, H.G.5
  • 65
    • 33646863941 scopus 로고    scopus 로고
    • The role of proline residues in the dynamics of transmembrane helices: The case of bacteriorhodopsin
    • A. Peralvarez-Marin, J.L. Bourdelande, E. Querol, and E. Padros The role of proline residues in the dynamics of transmembrane helices: the case of bacteriorhodopsin Mol Membr Biol 23 2006 127 135
    • (2006) Mol Membr Biol , vol.23 , pp. 127-135
    • Peralvarez-Marin, A.1    Bourdelande, J.L.2    Querol, E.3    Padros, E.4
  • 66
    • 0024297167 scopus 로고
    • Effects of amino acid substitutions in the F helix of bacteriorhodopsin. Low temperature ultraviolet/visible difference spectroscopy
    • P.L. Ahl, L.J. Stern, D. During, T. Mogi, H.G. Khorana, and K.J. Rothschild Effects of amino acid substitutions in the F helix of bacteriorhodopsin. Low temperature ultraviolet/visible difference spectroscopy J Biol Chem 263 1988 13594 13601
    • (1988) J Biol Chem , vol.263 , pp. 13594-13601
    • Ahl, P.L.1    Stern, L.J.2    During, D.3    Mogi, T.4    Khorana, H.G.5    Rothschild, K.J.6
  • 67
    • 0030866067 scopus 로고    scopus 로고
    • Ultraviolet resonance Raman spectra of Trp-182 and Trp-189 in bacteriorhodopsin: Novel information on the structure of Trp-182 and its steric interaction with retinal
    • S. Hashimoto, K. Obata, H. Takeuchi, R. Needleman, and J.K. Lanyi Ultraviolet resonance Raman spectra of Trp-182 and Trp-189 in bacteriorhodopsin: novel information on the structure of Trp-182 and its steric interaction with retinal Biochemistry 36 1997 11583 11590
    • (1997) Biochemistry , vol.36 , pp. 11583-11590
    • Hashimoto, S.1    Obata, K.2    Takeuchi, H.3    Needleman, R.4    Lanyi, J.K.5
  • 68
    • 0025157075 scopus 로고
    • Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82 - Ala and Asp-85 - Glu: The blue form is inactive in proton translocation
    • S. Subramaniam, T. Marti, and H.G. Khorana Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82 - Ala and Asp-85 - Glu: the blue form is inactive in proton translocation Proc Natl Acad Sci USA 87 1990 1013 1017
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1013-1017
    • Subramaniam, S.1    Marti, T.2    Khorana, H.G.3
  • 69
    • 0141817991 scopus 로고    scopus 로고
    • Spectroscopic and photochemical characterization of a deep ocean proteorhodopsin
    • W.W. Wang, O.A. Sineshchekov, E.N. Spudich, and J.L. Spudich Spectroscopic and photochemical characterization of a deep ocean proteorhodopsin J Biol Chem 278 2003 33985 33991
    • (2003) J Biol Chem , vol.278 , pp. 33985-33991
    • Wang, W.W.1    Sineshchekov, O.A.2    Spudich, E.N.3    Spudich, J.L.4
  • 71
    • 84869425632 scopus 로고    scopus 로고
    • Photoinduced proton release in proteorhodopsin at low pH: The possibility of a decrease in the pK(a) of Asp227
    • J. Tamogami, T. Kikukawa, T. Nara, K. Shimono, M. Demura, and N. Kamo Photoinduced proton release in proteorhodopsin at low pH: the possibility of a decrease in the pK(a) of Asp227 Biochemistry 51 2012 9290 9301
    • (2012) Biochemistry , vol.51 , pp. 9290-9301
    • Tamogami, J.1    Kikukawa, T.2    Nara, T.3    Shimono, K.4    Demura, M.5    Kamo, N.6
  • 72
    • 0026069154 scopus 로고
    • Development of hydrophobicity parameters to analyze proteins which bear posttranslational or cotranslational modifications
    • S.D. Black, and D.R. Mould Development of hydrophobicity parameters to analyze proteins which bear posttranslational or cotranslational modifications Anal Biochem 193 1991 72 82
    • (1991) Anal Biochem , vol.193 , pp. 72-82
    • Black, S.D.1    Mould, D.R.2
  • 75
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A Web-based environment for protein structure homology modelling
    • K. Arnold, L. Bordoli, J. Kopp, and T. Schwede The SWISS-MODEL workspace: a Web-based environment for protein structure homology modelling Bioinformatics 22 2006 195 201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 76
    • 18044397860 scopus 로고    scopus 로고
    • Mathematical expressions useful in the construction, description and evaluation of protein libraries
    • A.D. Bosley, and M. Ostermeier Mathematical expressions useful in the construction, description and evaluation of protein libraries Biomol Eng 22 2005 57 61
    • (2005) Biomol Eng , vol.22 , pp. 57-61
    • Bosley, A.D.1    Ostermeier, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.