메뉴 건너뛰기




Volumn 1757, Issue 8, 2006, Pages 1012-1018

Proton transfers in the bacteriorhodopsin photocycle

Author keywords

Bacteriorhodopsin; Hydrogen bonded chain; Proton release; Proton uptake; Retinal; X ray structure

Indexed keywords

BACTERIORHODOPSIN; WATER;

EID: 33748903643     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2005.11.003     Document Type: Review
Times cited : (190)

References (86)
  • 1
    • 3543033483 scopus 로고    scopus 로고
    • What is the real crystallographic structure of the L photointermediate of bacteriorhodopsin?
    • Lanyi J.K. What is the real crystallographic structure of the L photointermediate of bacteriorhodopsin?. Biochim. Biophys. Acta 1658 (2004) 14-22
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 14-22
    • Lanyi, J.K.1
  • 2
    • 85005688720 scopus 로고
    • The photocycles of bacteriorhodopsin
    • Lanyi J.K., and Varo G. The photocycles of bacteriorhodopsin. Isr. J. Chem. 35 (1995) 365-385
    • (1995) Isr. J. Chem. , vol.35 , pp. 365-385
    • Lanyi, J.K.1    Varo, G.2
  • 3
    • 0032455636 scopus 로고    scopus 로고
    • Understanding structure and function in the light-driven proton pump bacteriorhodopsin
    • Lanyi J.K. Understanding structure and function in the light-driven proton pump bacteriorhodopsin. J. Struct. Biol. 124 (1998) 164-178
    • (1998) J. Struct. Biol. , vol.124 , pp. 164-178
    • Lanyi, J.K.1
  • 4
    • 0032437382 scopus 로고    scopus 로고
    • Bacteriorhodopsin
    • Lanyi J.K. Bacteriorhodopsin. Int. Rev. Cytol. 187 (1999) 161-202
    • (1999) Int. Rev. Cytol. , vol.187 , pp. 161-202
    • Lanyi, J.K.1
  • 5
    • 0033382026 scopus 로고    scopus 로고
    • Progress toward an explicit mechanistic model for the light-driven pump, bacteriorhodopsin
    • Lanyi J.K. Progress toward an explicit mechanistic model for the light-driven pump, bacteriorhodopsin. FEBS Lett. 464 (1999) 103-107
    • (1999) FEBS Lett. , vol.464 , pp. 103-107
    • Lanyi, J.K.1
  • 6
    • 0034499002 scopus 로고    scopus 로고
    • Molecular mechanism of ion transport in bacteriorhodopsin: insights from crystallographic, spectroscopic, kinetic and mutational studies
    • Lanyi J.K. Molecular mechanism of ion transport in bacteriorhodopsin: insights from crystallographic, spectroscopic, kinetic and mutational studies. J. Phys. Chem., B 104 (2000) 11441-11448
    • (2000) J. Phys. Chem., B , vol.104 , pp. 11441-11448
    • Lanyi, J.K.1
  • 7
    • 0035313782 scopus 로고    scopus 로고
    • Proton pumps: mechanism of action and applications
    • Lanyi J.K., and Pohorille A. Proton pumps: mechanism of action and applications. Trends Biotechnol. 19 (2001) 140-144
    • (2001) Trends Biotechnol. , vol.19 , pp. 140-144
    • Lanyi, J.K.1    Pohorille, A.2
  • 8
    • 0035498344 scopus 로고    scopus 로고
    • X-ray crystallography of bacteriorhodopsin and its photointermediates: insights into the mechanism of proton transport
    • Lanyi J.K. X-ray crystallography of bacteriorhodopsin and its photointermediates: insights into the mechanism of proton transport. Biochemistry (Mosc.) 66 (2001) 1192-1196
    • (2001) Biochemistry (Mosc.) , vol.66 , pp. 1192-1196
    • Lanyi, J.K.1
  • 10
    • 0034499002 scopus 로고    scopus 로고
    • Molecular mechanism of ion transport in bacteriorhodopsin: insights from crystallographic, spectroscopic, kinetic, and mutational studies
    • Lanyi J.K. Molecular mechanism of ion transport in bacteriorhodopsin: insights from crystallographic, spectroscopic, kinetic, and mutational studies. J. Phys. Chem., B 104 (2003) 11441-11448
    • (2003) J. Phys. Chem., B , vol.104 , pp. 11441-11448
    • Lanyi, J.K.1
  • 11
    • 0346727449 scopus 로고    scopus 로고
    • Local-global conformational coupling in a heptahelical membrane protein: transport mechanism from crystal structures of the nine States in the bacteriorhodopsin photocycle
    • Lanyi J.K., and Schobert B. Local-global conformational coupling in a heptahelical membrane protein: transport mechanism from crystal structures of the nine States in the bacteriorhodopsin photocycle. Biochemistry 43 (2004) 3-8
    • (2004) Biochemistry , vol.43 , pp. 3-8
    • Lanyi, J.K.1    Schobert, B.2
  • 12
    • 2942556920 scopus 로고    scopus 로고
    • X-ray diffraction of bacteriorhodopsin photocycle intermediates
    • Lanyi J.K. X-ray diffraction of bacteriorhodopsin photocycle intermediates. Mol. Membr. Biol. 21 (2004) 143-150
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 143-150
    • Lanyi, J.K.1
  • 13
    • 33748885865 scopus 로고    scopus 로고
    • J.K. Lanyi, A structural view of proton transport in bacteriorhodopsin, in: M. Wikström (Ed.), Biophysical and structural aspects of bioenergetics, Royal Soc. Chem. U.K., in press.
  • 14
    • 0031021374 scopus 로고    scopus 로고
    • General concept for ion translocation by halobacterial retinal proteins: the isomerization/switch/transfer (IST) model
    • Haupts U., Tittor J., Bamberg E., and Oesterhelt D. General concept for ion translocation by halobacterial retinal proteins: the isomerization/switch/transfer (IST) model. Biochemistry 36 (1997) 2-7
    • (1997) Biochemistry , vol.36 , pp. 2-7
    • Haupts, U.1    Tittor, J.2    Bamberg, E.3    Oesterhelt, D.4
  • 15
    • 0032144042 scopus 로고    scopus 로고
    • The structure and mechanism of the family of retinal proteins from halophilic archaea
    • Oesterhelt D. The structure and mechanism of the family of retinal proteins from halophilic archaea. Curr. Opin. Struct. Biol. 8 (1998) 489-500
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 489-500
    • Oesterhelt, D.1
  • 16
    • 0034734239 scopus 로고    scopus 로고
    • Structures of photointermediates and their implications for the proton pump mechanism
    • Kataoka M., and Kamikubo H. Structures of photointermediates and their implications for the proton pump mechanism. Biochim. Biophys. Acta 1460 (2000) 166-176
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 166-176
    • Kataoka, M.1    Kamikubo, H.2
  • 17
    • 0034734254 scopus 로고    scopus 로고
    • Role of internal water molecules in bacteriorhodopsin
    • Kandori H. 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
  • 18
    • 0035498346 scopus 로고    scopus 로고
    • Proton transport mechanism of bacteriorhodopsin as revealed by site- specific mutagenesis and protein sequence variability
    • Brown L.S. Proton transport mechanism of bacteriorhodopsin as revealed by site- specific mutagenesis and protein sequence variability. Biochemistry (Mosc.) 66 (2001) 1249-1255
    • (2001) Biochemistry (Mosc.) , vol.66 , pp. 1249-1255
    • Brown, L.S.1
  • 19
    • 0036089699 scopus 로고    scopus 로고
    • Magnetic resonance studies of the bacteriorhodopsin pump cycle
    • Herzfeld J., and Lansing J.C. Magnetic resonance studies of the bacteriorhodopsin pump cycle. Annu. Rev. Biophys. Biomol. Struct. 31 (2002) 73-95
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 73-95
    • Herzfeld, J.1    Lansing, J.C.2
  • 21
    • 0041352147 scopus 로고    scopus 로고
    • X-ray crystallographic analysis of lipid-protein interactions in the bacteriorhodopsin purple membrane
    • Cartailler J.P., and Luecke H. X-ray crystallographic analysis of lipid-protein interactions in the bacteriorhodopsin purple membrane. Annu. Rev. Biophys. Biomol. Struct. 32 (2003) 285-310
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 285-310
    • Cartailler, J.P.1    Luecke, H.2
  • 23
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 A resolution
    • Belrhali H., Nollert P., Royant A., Menzel C., Rosenbusch J.P., Landau E.M., and Pebay-Peyroula E. Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 A resolution. Struct. Fold. Des 7 (1999) 909-917
    • (1999) Struct. Fold. Des , vol.7 , pp. 909-917
    • Belrhali, H.1    Nollert, P.2    Royant, A.3    Menzel, C.4    Rosenbusch, J.P.5    Landau, E.M.6    Pebay-Peyroula, E.7
  • 25
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex
    • Essen L., Siegert R., Lehmann W.D., and Oesterhelt D. Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 11673-11678
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11673-11678
    • Essen, L.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 26
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2. 3 angstrom resolution
    • Luecke H., Richter H.T., and Lanyi J.K. Proton transfer pathways in bacteriorhodopsin at 2. 3 angstrom resolution. Science 280 (1998) 1934-1937
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.T.2    Lanyi, J.K.3
  • 27
    • 0032143387 scopus 로고    scopus 로고
    • Proton translocation by bacteriorhodopsin and heme-copper oxidases
    • Wikstrom M. Proton translocation by bacteriorhodopsin and heme-copper oxidases. Curr. Opin. Struct. Biol. 8 (1998) 480-488
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 480-488
    • Wikstrom, M.1
  • 30
    • 0027244529 scopus 로고
    • Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle
    • Brown L.S., Bonet L., Needleman R., and Lanyi J.K. Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle. Biophys. J. 65 (1993) 124-130
    • (1993) Biophys. J. , vol.65 , pp. 124-130
    • Brown, L.S.1    Bonet, L.2    Needleman, R.3    Lanyi, J.K.4
  • 32
    • 0000559536 scopus 로고
    • a of the retinal protonated Schiff base in retinal proteins. A study with model compounds
    • a of the retinal protonated Schiff base in retinal proteins. A study with model compounds. J. Am. Chem. Soc. 115 (1993) 3772-3773
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3772-3773
    • Gat, Y.1    Sheves, M.2
  • 33
    • 0028134307 scopus 로고
    • The retinal Schiff base-counterion complex of bacteriorhodopsin: changed geometry during the photocycle is a cause of proton transfer to aspartate 85
    • Brown L.S., Gat Y., Sheves M., Yamazaki Y., Maeda A., Needleman R., and Lanyi J.K. The retinal Schiff base-counterion complex of bacteriorhodopsin: changed geometry during the photocycle is a cause of proton transfer to aspartate 85. Biochemistry 33 (1994) 12001-12011
    • (1994) Biochemistry , vol.33 , pp. 12001-12011
    • Brown, L.S.1    Gat, Y.2    Sheves, M.3    Yamazaki, Y.4    Maeda, A.5    Needleman, R.6    Lanyi, J.K.7
  • 34
    • 0036971196 scopus 로고    scopus 로고
    • Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal
    • Schobert B., Cupp-Vickery J., Hornak V., Smith S., and Lanyi J. Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal. J. Mol. Biol. 321 (2002) 715-726
    • (2002) J. Mol. Biol. , vol.321 , pp. 715-726
    • Schobert, B.1    Cupp-Vickery, J.2    Hornak, V.3    Smith, S.4    Lanyi, J.5
  • 35
    • 0037466289 scopus 로고    scopus 로고
    • Mechanism of proton transport in bacteriorhodopsin from crystallographic structures of the K, L, M-1, M-2, and M-2′ intermediates of the photocycle
    • Lanyi J.K., and Schobert B. Mechanism of proton transport in bacteriorhodopsin from crystallographic structures of the K, L, M-1, M-2, and M-2′ intermediates of the photocycle. J. Mol. Biol. 328 (2003) 439-450
    • (2003) J. Mol. Biol. , vol.328 , pp. 439-450
    • Lanyi, J.K.1    Schobert, B.2
  • 36
    • 0034734227 scopus 로고    scopus 로고
    • NMR probes of vectoriality in the proton-motive photocycle of bacteriorhodopsin: evidence for an 'electrostatic steering' mechanism
    • Herzfeld J., and Tounge B. NMR probes of vectoriality in the proton-motive photocycle of bacteriorhodopsin: evidence for an 'electrostatic steering' mechanism. Biochim. Biophys. Acta 1460 (2000) 95-105
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 95-105
    • Herzfeld, J.1    Tounge, B.2
  • 37
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution
    • Luecke H., Schobert B., Richter H.T., Cartailler J.P., and Lanyi J.K. Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution. Science 286 (1999) 255-261
    • (1999) Science , vol.286 , pp. 255-261
    • Luecke, H.1    Schobert, B.2    Richter, H.T.3    Cartailler, J.P.4    Lanyi, J.K.5
  • 40
    • 0346366810 scopus 로고    scopus 로고
    • Crystal structure of the L intermediate of bacteriorhodopsin: evidence for vertical translocation of a water molecule during the proton pumping cycle
    • Kouyama T., Nishikawa T., Tokuhisa T., and Okumura H. Crystal structure of the L intermediate of bacteriorhodopsin: evidence for vertical translocation of a water molecule during the proton pumping cycle. J. Mol. Biol. 335 (2004) 531-546
    • (2004) J. Mol. Biol. , vol.335 , pp. 531-546
    • Kouyama, T.1    Nishikawa, T.2    Tokuhisa, T.3    Okumura, H.4
  • 41
    • 0034632821 scopus 로고    scopus 로고
    • Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin
    • Royant A., Edman K., Ursby T., Pebay-Peyroula E., Landau E.M., and Neutze R. Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin. Nature 406 (2000) 645-648
    • (2000) Nature , vol.406 , pp. 645-648
    • Royant, A.1    Edman, K.2    Ursby, T.3    Pebay-Peyroula, E.4    Landau, E.M.5    Neutze, R.6
  • 43
    • 0037432333 scopus 로고    scopus 로고
    • Water molecule rearrangements around leu93 and trp182 in the formation of the L intermediate in bacteriorhodopsin's photocycle
    • Maeda A., Tomson F.L., Gennis R.B., Balashov S.P., and Ebrey T.G. Water molecule rearrangements around leu93 and trp182 in the formation of the L intermediate in bacteriorhodopsin's photocycle. Biochemistry 42 (2003) 2535-2541
    • (2003) Biochemistry , vol.42 , pp. 2535-2541
    • Maeda, A.1    Tomson, F.L.2    Gennis, R.B.3    Balashov, S.P.4    Ebrey, T.G.5
  • 44
    • 0344629882 scopus 로고    scopus 로고
    • Water-mediated hydrogen-bonded network on the cytoplasmic side of the Schiff base of the L photointermediate of bacteriorhodopsin
    • Maeda A., Herzfeld J., Belenky M., Needleman R., Gennis R.B., Balashov S.P., and Ebrey T.G. Water-mediated hydrogen-bonded network on the cytoplasmic side of the Schiff base of the L photointermediate of bacteriorhodopsin. Biochemistry 42 (2003) 14122-14129
    • (2003) Biochemistry , vol.42 , pp. 14122-14129
    • Maeda, A.1    Herzfeld, J.2    Belenky, M.3    Needleman, R.4    Gennis, R.B.5    Balashov, S.P.6    Ebrey, T.G.7
  • 45
    • 7744225102 scopus 로고    scopus 로고
    • Key role of electrostatic interactions in bacteriorhodopsin proton transfer
    • Bondar A.N., Fischer S., Smith J.C., Elstner M., and Suhai S. Key role of electrostatic interactions in bacteriorhodopsin proton transfer. J. Am. Chem. Soc. 126 (2004) 14668-14677
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 14668-14677
    • Bondar, A.N.1    Fischer, S.2    Smith, J.C.3    Elstner, M.4    Suhai, S.5
  • 46
    • 0034734246 scopus 로고    scopus 로고
    • Atomic resolution structures of bacteriorhodopsin photocycle intermediates: the role of discrete water molecules in the function of this light-driven ion pump
    • Luecke H. Atomic resolution structures of bacteriorhodopsin photocycle intermediates: the role of discrete water molecules in the function of this light-driven ion pump. Biochim. Biophys. Acta 1460 (2000) 133-156
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 133-156
    • Luecke, H.1
  • 47
    • 0342484454 scopus 로고    scopus 로고
    • Analogies between halorhodopsin and bacteriorhodopsin
    • Varo G. Analogies between halorhodopsin and bacteriorhodopsin. Biochim. Biophys. Acta 1460 (2000) 220-229
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 220-229
    • Varo, G.1
  • 48
    • 85005560634 scopus 로고
    • Structure and function in halorhodopsin
    • Oesterhelt D. Structure and function in halorhodopsin. Isr. J. Chem. 35 (1995) 475-494
    • (1995) Isr. J. Chem. , vol.35 , pp. 475-494
    • Oesterhelt, D.1
  • 50
    • 24944531254 scopus 로고    scopus 로고
    • Hydrogen-bonding alterations of the protonated Schiif base and a water molecule in the chloride pump of Natronobacter pharaonis
    • Shibata M., Muneda N., Sasaki T., Shimono K., Kamo N., Demura M., and Kandori H. Hydrogen-bonding alterations of the protonated Schiif base and a water molecule in the chloride pump of Natronobacter pharaonis. Biochemistry 44 (2005) 12279-12286
    • (2005) Biochemistry , vol.44 , pp. 12279-12286
    • Shibata, M.1    Muneda, N.2    Sasaki, T.3    Shimono, K.4    Kamo, N.5    Demura, M.6    Kandori, H.7
  • 52
    • 0030069626 scopus 로고    scopus 로고
    • Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release
    • Balashov S.P., Imasheva E.S., Govindjee R., and Ebrey T.G. Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release. Biophys. J. 70 (1996) 473-481
    • (1996) Biophys. J. , vol.70 , pp. 473-481
    • Balashov, S.P.1    Imasheva, E.S.2    Govindjee, R.3    Ebrey, T.G.4
  • 53
    • 0029665673 scopus 로고    scopus 로고
    • a's of asp-85 and glu-204 forms part of the reprotonation switch of bacteriorhodopsin
    • a's of asp-85 and glu-204 forms part of the reprotonation switch of bacteriorhodopsin. Biochemistry 35 (1996) 4054-4062
    • (1996) Biochemistry , vol.35 , pp. 4054-4062
    • Richter, H.T.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 54
    • 0028864699 scopus 로고
    • Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin
    • Brown L.S., Sasaki J., Kandori H., Maeda A., Needleman R., and Lanyi J.K. 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
  • 56
    • 0032492706 scopus 로고    scopus 로고
    • Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network
    • Rammelsberg R., Huhn G., Lubben M., and Gerwert K. Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network. Biochemistry 37 (1998) 5001-5009
    • (1998) Biochemistry , vol.37 , pp. 5001-5009
    • Rammelsberg, R.1    Huhn, G.2    Lubben, M.3    Gerwert, K.4
  • 57
    • 0035823064 scopus 로고    scopus 로고
    • pK(a) calculations suggest storage of an excess proton in a hydrogen-bonded water network in bacteriorhodopsin
    • Spassov V.Z., Luecke H., Gerwert K., and Bashford D. pK(a) calculations suggest storage of an excess proton in a hydrogen-bonded water network in bacteriorhodopsin. J. Mol. Biol. 312 (2001) 203-219
    • (2001) J. Mol. Biol. , vol.312 , pp. 203-219
    • Spassov, V.Z.1    Luecke, H.2    Gerwert, K.3    Bashford, D.4
  • 59
    • 0030040314 scopus 로고    scopus 로고
    • A model molecule of the hydrogen-bonded chain in the active site of bacteriorhodopsin
    • Brzezinski B., Urjasz H., and Zundel G. A model molecule of the hydrogen-bonded chain in the active site of bacteriorhodopsin. Biochem. Biophys. Res. Commun. 219 (1996) 273-276
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 273-276
    • Brzezinski, B.1    Urjasz, H.2    Zundel, G.3
  • 60
    • 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
    • Dioumaev A.K., Richter H.T., Brown L.S., Tanio M., Tuzi S., Saito H., Kimura Y., Needleman R., and Lanyi J.K. 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
    • (1998) Biochemistry , vol.37 , 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
  • 61
  • 62
    • 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
    • Lanyi J.K., and Schobert B. Crystallographic structure of the retinal and the protein after deprotonation of the Schiff base: the switch in the bacteriorhodopsin photocycle. J. Mol. Biol. 321 (2002) 727-737
    • (2002) J. Mol. Biol. , vol.321 , pp. 727-737
    • Lanyi, J.K.1    Schobert, B.2
  • 64
    • 0028023207 scopus 로고
    • pH-induced structural changes in bacteriorhodopsin studied by Fourier Transform Infrared Spectroscopy
    • Szaraz S., Oesterhelt D., and Ormos P. pH-induced structural changes in bacteriorhodopsin studied by Fourier Transform Infrared Spectroscopy. Biophys. J. 67 (1994) 1706-1712
    • (1994) Biophys. J. , vol.67 , pp. 1706-1712
    • Szaraz, S.1    Oesterhelt, D.2    Ormos, P.3
  • 65
    • 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 Asp96 and the retinal Schiff base
    • Schobert B., Brown L.S., and Lanyi J.K. Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between Asp96 and the retinal Schiff base. J. Mol. Biol. 330 (2003) 553-570
    • (2003) J. Mol. Biol. , vol.330 , pp. 553-570
    • Schobert, B.1    Brown, L.S.2    Lanyi, J.K.3
  • 66
    • 0033545872 scopus 로고    scopus 로고
    • a changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy
    • a changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 5498-5503
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5498-5503
    • Zscherp, C.1    Schlesinger, R.2    Tittor, J.3    Oesterhelt, D.4    Heberle, J.5
  • 67
    • 0034113865 scopus 로고    scopus 로고
    • On the protein residues that control the yield and kinetics of O(630) in the photocycle of bacteriorhodopsin
    • Li Q., Bressler S., Ovrutsky D., Ottolenghi M., Friedman N., and Sheves M. On the protein residues that control the yield and kinetics of O(630) in the photocycle of bacteriorhodopsin. Biophys. J. 78 (2000) 354-362
    • (2000) Biophys. J. , vol.78 , pp. 354-362
    • Li, Q.1    Bressler, S.2    Ovrutsky, D.3    Ottolenghi, M.4    Friedman, N.5    Sheves, M.6
  • 68
    • 0035949633 scopus 로고    scopus 로고
    • Coupling of the reisomerization of the retinal, proton uptake, and reprotonation of asp-96 in the n photointermediate of bacteriorhodopsin
    • Dioumaev A.K., Brown L.S., Needleman R., and Lanyi J.K. Coupling of the reisomerization of the retinal, proton uptake, and reprotonation of asp-96 in the n photointermediate of bacteriorhodopsin. Biochemistry 40 (2001) 11308-11317
    • (2001) Biochemistry , vol.40 , pp. 11308-11317
    • Dioumaev, A.K.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 69
    • 0029864761 scopus 로고    scopus 로고
    • a of the retinal Schiff base during the photocycle of bacteriorhodopsin
    • a of the retinal Schiff base during the photocycle of bacteriorhodopsin. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 1731-1734
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1731-1734
    • Brown, L.S.1    Lanyi, J.K.2
  • 70
    • 17444439064 scopus 로고    scopus 로고
    • Proton transport through water-filled carbon nanotubes
    • Dellago C., Naor M.M., and Hummer G. Proton transport through water-filled carbon nanotubes. Phys. Rev. Lett. 90 (2003) 105902
    • (2003) Phys. Rev. Lett. , vol.90 , pp. 105902
    • Dellago, C.1    Naor, M.M.2    Hummer, G.3
  • 71
    • 0026332339 scopus 로고
    • Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base
    • Cao Y., Varo G., Chang M., Ni B., Needleman R., and Lanyi J.K. Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base. Biochemistry 30 (1991) 10972-10979
    • (1991) Biochemistry , vol.30 , pp. 10972-10979
    • Cao, Y.1    Varo, G.2    Chang, M.3    Ni, B.4    Needleman, R.5    Lanyi, J.K.6
  • 72
    • 0024317089 scopus 로고
    • Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin
    • Otto H., Marti T., Holz M., Mogi T., Lindau M., Khorana H.G., and Heyn M.P. Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 9228-9232
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 9228-9232
    • Otto, H.1    Marti, T.2    Holz, M.3    Mogi, T.4    Lindau, M.5    Khorana, H.G.6    Heyn, M.P.7
  • 74
    • 0025011266 scopus 로고
    • Kinetic optimization of bacteriorhodopsin by aspartic acid 96 as an internal proton donor
    • Miller A., and Oesterhelt D. Kinetic optimization of bacteriorhodopsin by aspartic acid 96 as an internal proton donor. Biochim. Biophys. Acta 1020 (1990) 57-64
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 57-64
    • Miller, A.1    Oesterhelt, D.2
  • 75
    • 0032516460 scopus 로고    scopus 로고
    • Partitioning of free energy gain between the photoisomerized retinal and the protein in bacteriorhodopsin
    • Dioumaev A.K., Brown L.S., Needleman R., and Lanyi J.K. Partitioning of free energy gain between the photoisomerized retinal and the protein in bacteriorhodopsin. Biochemistry 37 (1998) 9889-9893
    • (1998) Biochemistry , vol.37 , pp. 9889-9893
    • Dioumaev, A.K.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 76
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • Subramaniam S., and Henderson R. Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature 406 (2000) 653-657
    • (2000) Nature , vol.406 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 77
    • 0030665489 scopus 로고    scopus 로고
    • Mechanism of proton entry into the cytoplasmic section of the proton-conducting channel of bacteriorhodopsin
    • Checover S., Nachliel E., Dencher N.A., and Gutman M. Mechanism of proton entry into the cytoplasmic section of the proton-conducting channel of bacteriorhodopsin. Biochemistry 36 (1997) 13919-13928
    • (1997) Biochemistry , vol.36 , pp. 13919-13928
    • Checover, S.1    Nachliel, E.2    Dencher, N.A.3    Gutman, M.4
  • 80
    • 0033602998 scopus 로고    scopus 로고
    • Functional roles of aspartic acid residues at the cytoplasmic surface of bacteriorhodopsin
    • Brown L.S., Needleman R., and Lanyi J.K. Functional roles of aspartic acid residues at the cytoplasmic surface of bacteriorhodopsin. Biochemistry 38 (1999) 6855-6861
    • (1999) Biochemistry , vol.38 , pp. 6855-6861
    • Brown, L.S.1    Needleman, R.2    Lanyi, J.K.3
  • 81
    • 0031738407 scopus 로고    scopus 로고
    • Kinetic and thermodynamic study of the bacteriorhodopsin photocycle over a wide pH range
    • Ludmann K., Gergely C., and Varo G. Kinetic and thermodynamic study of the bacteriorhodopsin photocycle over a wide pH range. Biophys. J. 75 (1998) 3110-3119
    • (1998) Biophys. J. , vol.75 , pp. 3110-3119
    • Ludmann, K.1    Gergely, C.2    Varo, G.3
  • 82
    • 0025820289 scopus 로고
    • Thermodynamics and energy coupling in the bacteriorhodopsin photocycle
    • Varo G., and Lanyi J.K. Thermodynamics and energy coupling in the bacteriorhodopsin photocycle. Biochemistry 30 (1991) 5016-5022
    • (1991) Biochemistry , vol.30 , pp. 5016-5022
    • Varo, G.1    Lanyi, J.K.2
  • 83
    • 0029969750 scopus 로고    scopus 로고
    • Relationship of retinal configuration and internal proton transfer at the end of the bacteriorhodopsin photocycle
    • Richter H.T., Needleman R., Kandori H., Maeda A., and Lanyi J.K. Relationship of retinal configuration and internal proton transfer at the end of the bacteriorhodopsin photocycle. Biochemistry 35 (1996) 15461-15466
    • (1996) Biochemistry , vol.35 , pp. 15461-15466
    • Richter, H.T.1    Needleman, R.2    Kandori, H.3    Maeda, A.4    Lanyi, J.K.5
  • 85
    • 0033520062 scopus 로고    scopus 로고
    • Fourier transform infrared spectra of a late intermediate of the bacteriorhodopsin photocycle suggest transient protonation of Asp-212
    • Dioumaev A.K., Brown L.S., Needleman R., and Lanyi J.K. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.