메뉴 건너뛰기




Volumn 46, Issue 18, 2007, Pages 5365-5373

FTIR study of the retinal Schiff base and internal water molecules of proteorhodopsin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN (BR); PROTEORHODOPSIN; RETINAL PHOTOISOMERIZATION;

EID: 34248193410     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700143g     Document Type: Article
Times cited : (68)

References (44)
  • 1
    • 0032987196 scopus 로고    scopus 로고
    • Closing in on bacteriorhodopsin: Progress in understanding the molecules
    • Haupts, U., Tittor, J., and Oesterhelt, D. (1999) Closing in on bacteriorhodopsin: progress in understanding the molecules, Annu. Rev. Biophys. Biomol. Struct. 28, 367-399.
    • (1999) Annu. Rev. Biophys. Biomol. Struct , vol.28 , pp. 367-399
    • Haupts, U.1    Tittor, J.2    Oesterhelt, D.3
  • 2
    • 0034499002 scopus 로고    scopus 로고
    • Molecular mechanism of ion transport in bacteriorhodopsin: Insights from crystallographic, spectroscopic, kinetic, and mutational studies
    • Lanyi, J. K. (2000) Molecular mechanism of ion transport in bacteriorhodopsin: insights from crystallographic, spectroscopic, kinetic, and mutational studies, J. Phys. Chem. B 104, 11441-11448.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 11441-11448
    • Lanyi, J.K.1
  • 3
    • 0034734254 scopus 로고    scopus 로고
    • Role of internal water molecules in bacteriorhodopsin
    • Kandori, H. (2000) Role of internal water molecules in bacteriorhodopsin, Biochim. Biophys. Acta 1460, 177-191.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 177-191
    • Kandori, H.1
  • 4
    • 0033529279 scopus 로고    scopus 로고
    • The nop-1 gene of neurospora crassa encodes a seven transmembrane helix retinal-binding protein homologous to archaeal rhodopsins
    • Bieszke, J. A., Braun, E. L., Bean, L. E., Kang, S., Natvig, D. O., and Borkovich, K. A. (1999) The nop-1 gene of neurospora crassa encodes a seven transmembrane helix retinal-binding protein homologous to archaeal rhodopsins, Proc. Natl. Acad. Sci. U.S.A. 96, 8034-8039.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 8034-8039
    • Bieszke, J.A.1    Braun, E.L.2    Bean, L.E.3    Kang, S.4    Natvig, D.O.5    Borkovich, K.A.6
  • 5
    • 0037173051 scopus 로고    scopus 로고
    • Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamydomonas reinhardtii
    • Sineshchekov, O. A., Jung, K. H., and Spudich, J. L. (2002) Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamydomonas reinhardtii, Proc. Natl. Acad. Sci. U.S.A. 99, 8689-8694.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 8689-8694
    • Sineshchekov, O.A.1    Jung, K.H.2    Spudich, J.L.3
  • 7
    • 0037346546 scopus 로고    scopus 로고
    • Demonstration of a sensory rhodopsin in eubacteria
    • Jung, K. H., Trivedi, V. D., and Spudich, J. L. (2003) Demonstration of a sensory rhodopsin in eubacteria, Mol. Microbiol. 47, 1513-1522.
    • (2003) Mol. Microbiol , vol.47 , pp. 1513-1522
    • Jung, K.H.1    Trivedi, V.D.2    Spudich, J.L.3
  • 8
    • 33745114416 scopus 로고    scopus 로고
    • Bacteriorhodopsin-like proteins of eubacteria and fungi: The extent of conservation of the haloarchaeal proton-pumping mechanism
    • Brown, L. S., and Jung, K. H. (2006) Bacteriorhodopsin-like proteins of eubacteria and fungi: the extent of conservation of the haloarchaeal proton-pumping mechanism, Photochem. Photobiol. Sci. 5, 538-546.
    • (2006) Photochem. Photobiol. Sci , vol.5 , pp. 538-546
    • Brown, L.S.1    Jung, K.H.2
  • 14
    • 0038390509 scopus 로고    scopus 로고
    • Proton transport by proteorhodopsin requires that the retinal schiff base counterion Asp-97 be anionic
    • Dioumaev, A. K., Wang, J. M., Balint, Z., Varo, G., and Lanyi, J. K. (2003) Proton transport by proteorhodopsin requires that the retinal schiff base counterion Asp-97 be anionic, Biochemistry 42, 6582-6587.
    • (2003) Biochemistry , vol.42 , pp. 6582-6587
    • Dioumaev, A.K.1    Wang, J.M.2    Balint, Z.3    Varo, G.4    Lanyi, J.K.5
  • 15
    • 3242801403 scopus 로고    scopus 로고
    • Light-induced intramolecular charge movement in microbial rhodopsins in intact E. coli cells
    • Sineshchekov, O. A., and Spudich, J. L. (2004) Light-induced intramolecular charge movement in microbial rhodopsins in intact E. coli cells, Biophys. J. 3, 548-554.
    • (2004) Biophys. J , vol.3 , pp. 548-554
    • Sineshchekov, O.A.1    Spudich, J.L.2
  • 16
    • 0038636606 scopus 로고    scopus 로고
    • The photochemical reaction cycle of proteorhodopsm at low pH
    • Lakatos, M., Lanyi, J. K., Szakacs, J., and Varo, G. (2003) The photochemical reaction cycle of proteorhodopsm at low pH, Biophys. J. 84, 3252-3256.
    • (2003) Biophys. J , vol.84 , pp. 3252-3256
    • Lakatos, M.1    Lanyi, J.K.2    Szakacs, J.3    Varo, G.4
  • 17
    • 0037304406 scopus 로고    scopus 로고
    • Characterization of the photochemical reaction cycle of proteorhodopsin
    • Varo, G., Brown, L. S., Lakatos, M., and Lanyi, J. K. (2003) Characterization of the photochemical reaction cycle of proteorhodopsin, Biophys. J. 84, 1202-1207.
    • (2003) Biophys. J , vol.84 , pp. 1202-1207
    • Varo, G.1    Brown, L.S.2    Lakatos, M.3    Lanyi, J.K.4
  • 18
    • 0036821737 scopus 로고    scopus 로고
    • Internal water molecules of archaeal rhodopsins
    • Furutani, Y., and Kandori, H. (2002) Internal water molecules of archaeal rhodopsins, Mol. Membr. Biol. 19, 257-265.
    • (2002) Mol. Membr. Biol , vol.19 , pp. 257-265
    • Furutani, Y.1    Kandori, H.2
  • 19
    • 0034731017 scopus 로고    scopus 로고
    • Direct observation of the bridged water stretching vibrations inside a protein
    • Kandori, H., and Shichida, Y. (2000) Direct observation of the bridged water stretching vibrations inside a protein, J. Am. Chem. Soc. 122, 11745-11746.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 11745-11746
    • Kandori, H.1    Shichida, Y.2
  • 20
    • 0242362271 scopus 로고    scopus 로고
    • Water molecules in the schiff base region of bacteriorhodopsin
    • Shibata, M., Tanimoto, T., and Kandori, H. (2003) Water molecules in the schiff base region of bacteriorhodopsin, J. Am. Chem. Soc. 125, 13312-13313.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 13312-13313
    • Shibata, M.1    Tanimoto, T.2    Kandori, H.3
  • 21
    • 18844385503 scopus 로고    scopus 로고
    • FTIR studies of internal water molecules in the Schiff base region of bacteriorhodopsin
    • Shibata, M., and Kandori, H. (2005) FTIR studies of internal water molecules in the Schiff base region of bacteriorhodopsin, Biochemistry 44, 7406-7413.
    • (2005) Biochemistry , vol.44 , pp. 7406-7413
    • Shibata, M.1    Kandori, H.2
  • 23
    • 0034321020 scopus 로고    scopus 로고
    • Proton transfer in bacteriorhodopsin: Structure, excitation, IR spectra, and potential energy surface analyses by an ab initio QM/MM method
    • Hayashi, S., and Ohmine, I. (2000) Proton transfer in bacteriorhodopsin: structure, excitation, IR spectra, and potential energy surface analyses by an ab initio QM/MM method, J. Phys. Chem. B 104, 10678-10691.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 10678-10691
    • Hayashi, S.1    Ohmine, I.2
  • 24
    • 24944531148 scopus 로고    scopus 로고
    • Strongly hydrogen-bonded water molecules in the Schiff base region of rhodopsins
    • Furutani, Y., Shibata, M., and Kandori, H. (2005) Strongly hydrogen-bonded water molecules in the Schiff base region of rhodopsins, Photochem. Photobiol. Sci. 4, 661-666.
    • (2005) Photochem. Photobiol. Sci , vol.4 , pp. 661-666
    • Furutani, Y.1    Shibata, M.2    Kandori, H.3
  • 25
    • 33646763173 scopus 로고    scopus 로고
    • Strongly hydrogen-bonded water molecule is observed only in the alkaline form of proteorhodopsin
    • Furutani, Y., Ikeda, D., Shibata, M., and Kandori, H. (2006) Strongly hydrogen-bonded water molecule is observed only in the alkaline form of proteorhodopsin, Chem. Phys. 324, 705-708.
    • (2006) Chem. Phys , vol.324 , pp. 705-708
    • Furutani, Y.1    Ikeda, D.2    Shibata, M.3    Kandori, H.4
  • 26
    • 3142779894 scopus 로고    scopus 로고
    • Structural changes in the photoactive site of proteorhodopsin during the primary photoreaction
    • Bergo, V., Amsden, J. J., Spudich, E. N., Spudich, J. L., and Rothschild, K. J. (2004) Structural changes in the photoactive site of proteorhodopsin during the primary photoreaction, Biochemistry 43, 9075-9083.
    • (2004) Biochemistry , vol.43 , pp. 9075-9083
    • Bergo, V.1    Amsden, J.J.2    Spudich, E.N.3    Spudich, J.L.4    Rothschild, K.J.5
  • 28
    • 14344261575 scopus 로고    scopus 로고
    • Structural changes of the complex between pharaonis phoborhodopsin and its cognate transducer upon formation of the M photointermediate
    • Furutani, Y., Kamada, K., Sudo, Y., Shimono, K., Kamo, N., and Kandori, H. (2005) Structural changes of the complex between pharaonis phoborhodopsin and its cognate transducer upon formation of the M photointermediate, Biochemistry 44, 2909-2915.
    • (2005) Biochemistry , vol.44 , pp. 2909-2915
    • Furutani, Y.1    Kamada, K.2    Sudo, Y.3    Shimono, K.4    Kamo, N.5    Kandori, H.6
  • 29
    • 0345492028 scopus 로고    scopus 로고
    • Hydrogen bonding alteration of Thr-204 in the complex between pharaonis phoborhodopsin and its transducer protein
    • Sudo, Y., Furutani, Y., Shimono, K., Kamo, N., and Kandori, H. (2003) Hydrogen bonding alteration of Thr-204 in the complex between pharaonis phoborhodopsin and its transducer protein, Biochemistry 42, 14166-14172.
    • (2003) Biochemistry , vol.42 , pp. 14166-14172
    • Sudo, Y.1    Furutani, Y.2    Shimono, K.3    Kamo, N.4    Kandori, H.5
  • 30
    • 23844528739 scopus 로고    scopus 로고
    • Formation of a long-lived photoproduct with a deprotonated Schiff base in proteorhodopsin, and its enhancement by mutation of Asp227
    • Imasheva, E. S., Shimono, K., Balashov, S. P., Wang, J. M., Zadok, U., Sheves, M., Kamo, N., and Lanyi, J. K. (2005) Formation of a long-lived photoproduct with a deprotonated Schiff base in proteorhodopsin, and its enhancement by mutation of Asp227, Biochemistry 44, 10828-10838.
    • (2005) Biochemistry , vol.44 , pp. 10828-10838
    • Imasheva, E.S.1    Shimono, K.2    Balashov, S.P.3    Wang, J.M.4    Zadok, U.5    Sheves, M.6    Kamo, N.7    Lanyi, J.K.8
  • 31
    • 3342894772 scopus 로고    scopus 로고
    • FTIR spectroscopy of the K photointermediate of neurospora rhodopsin: Structural changes of the retinal, protein, and water molecules after photoisomerization
    • Furutani, Y., Bezerra, A. G., Jr., Waschuk, S., Sumii, M., Brown, L. S., and Kandori, H. (2004) FTIR spectroscopy of the K photointermediate of neurospora rhodopsin: structural changes of the retinal, protein, and water molecules after photoisomerization, Biochemistry 43, 9636-9646.
    • (2004) Biochemistry , vol.43 , pp. 9636-9646
    • Furutani, Y.1    Bezerra Jr., A.G.2    Waschuk, S.3    Sumii, M.4    Brown, L.S.5    Kandori, H.6
  • 32
    • 0024024413 scopus 로고
    • Aspartic acid substitutions affect proton translocation by bacteriorhodopsin
    • Mogi, T., Stern, L. J., Marti, T., Chao, B. H., and Khorana, H. G. (1988) Aspartic acid substitutions affect proton translocation by bacteriorhodopsin, Proc. Natl. Acad. Sci. U.S.A. 85, 4148-4152.
    • (1988) Proc. Natl. Acad. Sci. U.S.A , vol.85 , pp. 4148-4152
    • Mogi, T.1    Stern, L.J.2    Marti, T.3    Chao, B.H.4    Khorana, H.G.5
  • 34
    • 0042233486 scopus 로고    scopus 로고
    • Resonance Raman characterization of proteorhodopsin's chromophore environment
    • Krebs, R. A., Dunmire, D., Partha, R., and Braiman, M. S. (2003) Resonance Raman characterization of proteorhodopsin's chromophore environment, J. Phys. Chem. B 107, 7877-7883.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 7877-7883
    • Krebs, R.A.1    Dunmire, D.2    Partha, R.3    Braiman, M.S.4
  • 36
    • 33749364966 scopus 로고    scopus 로고
    • Assignment of the hydrogen-out-of-plane vibrations of the retinal chromophore in the K intermediate of Pharaonis phoborhodopsin
    • Furutani, Y., Sudo, Y., Wada, A., Ito, M., Shimono, K., and Kandori, H. (2006) Assignment of the hydrogen-out-of-plane vibrations of the retinal chromophore in the K intermediate of Pharaonis phoborhodopsin, Biochemistry 45, 11836-11843.
    • (2006) Biochemistry , vol.45 , pp. 11836-11843
    • Furutani, Y.1    Sudo, Y.2    Wada, A.3    Ito, M.4    Shimono, K.5    Kandori, H.6
  • 37
    • 0023228884 scopus 로고
    • Factors affecting the C=N stretching in protonated retinal schiff base: A model study for bacteriorhodopsin and visual pigments
    • Baasov, T., Friedman, N., and Sheves, M. (1987) Factors affecting the C=N stretching in protonated retinal schiff base: a model study for bacteriorhodopsin and visual pigments, Biochemistry 26, 3210-3217.
    • (1987) Biochemistry , vol.26 , pp. 3210-3217
    • Baasov, T.1    Friedman, N.2    Sheves, M.3
  • 38
    • 0037076526 scopus 로고    scopus 로고
    • Vibrational frequency and dipolar orientation of the protonated Schiff base in bacteriorhodopsin before and after photoisomerization
    • Kandori, H., Belenly, M., and Herzfeld, J. (2002) Vibrational frequency and dipolar orientation of the protonated Schiff base in bacteriorhodopsin before and after photoisomerization, Biochemistry 41, 6026-6031.
    • (2002) Biochemistry , vol.41 , pp. 6026-6031
    • Kandori, H.1    Belenly, M.2    Herzfeld, J.3
  • 41
    • 0025873898 scopus 로고
    • Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation
    • Marti, T., Otto, H., Mogi, T., Rosselet, S. J., Heyn, M. P., and Khorana, H. G. (1990) Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation, J. Biol. Chem. 266, 6919-6927.
    • (1990) 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
  • 42
    • 0041320967 scopus 로고    scopus 로고
    • Molecular dynamics simulation of bacteriorhodospin's photoisomerization using ab initio forces for the excited chromophore
    • Hayashi, S., Tajkhorshid, E., and Schulten, K. (2003) Molecular dynamics simulation of bacteriorhodospin's photoisomerization using ab initio forces for the excited chromophore, Biophys. J. 85, 1440-1449.
    • (2003) Biophys. J , vol.85 , pp. 1440-1449
    • Hayashi, S.1    Tajkhorshid, E.2    Schulten, K.3
  • 43
    • 1042288283 scopus 로고    scopus 로고
    • Selectivity of retinal photoisomerization in proteorhodopsin is controlled by aspartic acid 227
    • Imasheva, E. S., Balashov, S. P., Wang, J. M., Dioumaev, A. K., and Lanyi, J. K. (2004) Selectivity of retinal photoisomerization in proteorhodopsin is controlled by aspartic acid 227, Biochemistry 43, 1648-1655.
    • (2004) Biochemistry , vol.43 , pp. 1648-1655
    • Imasheva, E.S.1    Balashov, S.P.2    Wang, J.M.3    Dioumaev, A.K.4    Lanyi, J.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.