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Volumn 72, Issue 2 I, 1997, Pages 886-898

Mutation of a surface residue, lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin; guanidine hydrochloride restores it

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN;

EID: 0031013660     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78723-X     Document Type: Article
Times cited : (24)

References (46)
  • 1
    • 0342575131 scopus 로고    scopus 로고
    • Restoring the photocycle and proton pumping in the mutant R82A of bacteriorhodopsin by guanidinium hydrochloride or a second mutation on the cytoplasmic surface
    • Alexiev, U., M. P. Krebs, R. Mollaaghababa, H. G. Khorana, and M. P. Heyn. 1996. Restoring the photocycle and proton pumping in the mutant R82A of bacteriorhodopsin by guanidinium hydrochloride or a second mutation on the cytoplasmic surface. Biophys. J. 70:A107.
    • (1996) Biophys. J. , vol.70
    • Alexiev, U.1    Krebs, M.P.2    Mollaaghababa, R.3    Khorana, H.G.4    Heyn, M.P.5
  • 2
    • 0028098029 scopus 로고
    • Surface charge of bacteriorhodopsin detected with covalently bound pH indicators at selected extracellular and cytoplasmic sites
    • Alexiev, U., T. Marti, M. P. Heyn, H. G. Khorana, and, P. Scherrer. 1994a. Surface charge of bacteriorhodopsin detected with covalently bound pH indicators at selected extracellular and cytoplasmic sites. Biochemistry. 33:298-306.
    • (1994) Biochemistry , vol.33 , pp. 298-306
    • Alexiev, U.1    Marti, T.2    Heyn, M.P.3    Khorana, H.G.4    Scherrer, P.5
  • 3
    • 0027940310 scopus 로고
    • Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 2. Rotational orientation of helices D and E and kinetic correlation between M formation and proton release in bacteriorhodopsin micelles
    • Alexiev, U., T. Marti, M. P. Heyn, H. G. Khorana, and P. Scherrer. 1994b. Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 2. Rotational orientation of helices D and E and kinetic correlation between M formation and proton release in bacteriorhodopsin micelles. Biochemistry. 33:13693-13699.
    • (1994) Biochemistry , vol.33 , pp. 13693-13699
    • Alexiev, U.1    Marti, T.2    Heyn, M.P.3    Khorana, H.G.4    Scherrer, P.5
  • 4
    • 0025346254 scopus 로고
    • Transmembrane protein structure: Spin labelling of bacteriorhodopsin mutants
    • Altenbach, C., T. Marti, H. G. Khorana, and W. L. Hubbell. 1990. Transmembrane protein structure: spin labelling of bacteriorhodopsin mutants. Science. 248:1088-1092.
    • (1990) Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.L.4
  • 5
    • 0025740089 scopus 로고
    • Red shift of the purple membrane absorption band and the deprotonation of tyrosine residues at high pH
    • Balashov, S. P., R. Govindjee, and T. G. Ebrey. 1991. Red shift of the purple membrane absorption band and the deprotonation of tyrosine residues at high pH. Biophys. J. 60:475-490.
    • (1991) Biophys. J. , vol.60 , pp. 475-490
    • Balashov, S.P.1    Govindjee, R.2    Ebrey, T.G.3
  • 7
    • 0027453982 scopus 로고
    • Effect of the arginine-82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release, and the photochemical cycle
    • Balashov, S. P., R. Govindjee, M. Kono, E. Imasheva, E. Lukashev, T. G. Ebrey, R. K. Crouch, D. R. Menick, and Y. Feng. 1993. Effect of the arginine-82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release, and the photochemical cycle. Biochemistry. 32: 10331-10343.
    • (1993) Biochemistry , vol.32 , pp. 10331-10343
    • Balashov, S.P.1    Govindjee, R.2    Kono, M.3    Imasheva, E.4    Lukashev, E.5    Ebrey, T.G.6    Crouch, R.K.7    Menick, D.R.8    Feng, Y.9
  • 8
    • 0030069626 scopus 로고    scopus 로고
    • Titration of aspartate-85 in bacteriorhodopsin: What it says about chromophore isomerization and proton release
    • Balashov, S. P., E. S. Imasheva, R. Govindjee, and T. G. Ebrey. 1996. Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release. Biophys. J. 70:473-481.
    • (1996) Biophys. J. , vol.70 , pp. 473-481
    • Balashov, S.P.1    Imasheva, E.S.2    Govindjee, R.3    Ebrey, T.G.4
  • 9
    • 0028864699 scopus 로고
    • Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin
    • Brown, L. S., J. Sasaki, H. Kandori, A. Maeda, R. Needleman, and J. K. Lanyi. 1995. Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin. J. Biol. Chem. 270: 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
  • 10
    • 0027386107 scopus 로고
    • Relationship of proton uptake on the cytoplasmic surface and the reisomerization of the retinal in the bacteriorhodopsin photocycle: An attempt to study the complex kinetics of the protons and the N and O intermediates
    • Cao, Y., L. S. Brown, R. Needleman, and J. K. Lanyi. 1993. Relationship of proton uptake on the cytoplasmic surface and the reisomerization of the retinal in the bacteriorhodopsin photocycle: an attempt to study the complex kinetics of the protons and the N and O intermediates. Biochemistry. 32:10239-10248.
    • (1993) Biochemistry , vol.32 , pp. 10239-10248
    • Cao, Y.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 11
    • 0016811990 scopus 로고
    • Flash photometric experiments on the photochemical cycle of bacteriorhodopsin
    • Dencher, N., and M. Wilms. 1975. Flash photometric experiments on the photochemical cycle of bacteriorhodopsin. Biophys. Struct Mech. 1:259-271.
    • (1975) Biophys. Struct Mech. , vol.1 , pp. 259-271
    • Dencher, N.1    Wilms, M.2
  • 13
    • 0002979180 scopus 로고
    • Light energy transduction in bacteriorhodopsin
    • M. Jackson, editor. CRC Press, Boca Raton, FL
    • Ebrey, T. G. 1993. Light energy transduction in bacteriorhodopsin. In Thermodynamics of Membranes, Receptors and Channels. M. Jackson, editor. CRC Press, Boca Raton, FL. 353-387.
    • (1993) Thermodynamics of Membranes, Receptors and Channels , pp. 353-387
    • Ebrey, T.G.1
  • 14
    • 0018635144 scopus 로고
    • Chromophore equilibria in bacteriorhodopsin
    • Fischer, U., and D. Oesterhelt. 1979. Chromophore equilibria in bacteriorhodopsin. Biophys. J. 28:211-230.
    • (1979) Biophys. J. , vol.28 , pp. 211-230
    • Fischer, U.1    Oesterhelt, D.2
  • 15
    • 0025034111 scopus 로고
    • Quantum efficiency of the photochemical cycle of bacteriorhodopsin
    • Govindjee, R., S. P. Balashov, and T. G. Ebrey. 1990. Quantum efficiency of the photochemical cycle of bacteriorhodopsin. Biophys. J. 58: 597-608.
    • (1990) Biophys. J. , vol.58 , pp. 597-608
    • Govindjee, R.1    Balashov, S.P.2    Ebrey, T.G.3
  • 16
    • 0028946790 scopus 로고
    • Effects of substitution of tyrosine 57 with asparagine and phenylalanine on the properties of bacteriorhodopsin
    • Govindjee, R., M. Kono, S. P. Balashov, E. Imasheva, M. Sheves, and T. G. Ebrey. 1995. Effects of substitution of tyrosine 57 with asparagine and phenylalanine on the properties of bacteriorhodopsin. Biochemistry. 34:4828-4838.
    • (1995) Biochemistry , vol.34 , pp. 4828-4838
    • Govindjee, R.1    Kono, M.2    Balashov, S.P.3    Imasheva, E.4    Sheves, M.5    Ebrey, T.G.6
  • 19
  • 20
    • 0025608977 scopus 로고
    • Bacteriorhodopsin in ice: Accelerated proton transfer from the purple membrane surface
    • Heberle, J., and N. A. Dencher. 1990. Bacteriorhodopsin in ice: accelerated proton transfer from the purple membrane surface. FEBS Lett. 277: 277-280.
    • (1990) FEBS Lett. , vol.277 , pp. 277-280
    • Heberle, J.1    Dencher, N.A.2
  • 21
    • 0026725522 scopus 로고
    • Surface-bound probes monitor proton translocation and surface potential changes during the bacteriorhodopsin photocycle
    • Heberle, J., and N. A. Dencher. 1992. Surface-bound probes monitor proton translocation and surface potential changes during the bacteriorhodopsin photocycle. Proc. Natl. Acad. Sci. USA. 89:5996-6000.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5996-6000
    • Heberle, J.1    Dencher, N.A.2
  • 22
    • 0028258544 scopus 로고
    • Molecular dynamics study of bacteriorhodopsin and artificial pigments
    • Humphrey, W., I. Logunov, K. Schulten, and M. Sheves. 1994. Molecular dynamics study of bacteriorhodopsin and artificial pigments. Biochemistry. 33:3668-3678.
    • (1994) Biochemistry , vol.33 , pp. 3668-3678
    • Humphrey, W.1    Logunov, I.2    Schulten, K.3    Sheves, M.4
  • 23
    • 0027394224 scopus 로고
    • Two light-transducing membrane proteins: Bacteriorhodopsin and the mammalian rhodopsin
    • Khorana, H. G. 1993. Two light-transducing membrane proteins: bacteriorhodopsin and the mammalian rhodopsin. Proc. Natl Acad. Sci. USA. 90:1166-1171.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1166-1171
    • Khorana, H.G.1
  • 24
    • 0027362929 scopus 로고
    • H dependence of light-induced proton release by bacteriorhodopsin
    • Kono, M., S. Misra, and T. G. Ebrey. 1993. pH dependence of light-induced proton release by bacteriorhodopsin. FEBS Lett. 331:31-34.
    • (1993) FEBS Lett. , vol.331 , pp. 31-34
    • Kono, M.1    Misra, S.2    Ebrey, T.G.3
  • 25
    • 0027769837 scopus 로고
    • Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin
    • Lanyi, J. K. 1993. Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin. Biochim. Biophys. Acta Bioenerg. 1183:241-261.
    • (1993) Biochim. Biophys. Acta Bioenerg. , vol.1183 , pp. 241-261
    • Lanyi, J.K.1
  • 26
  • 28
    • 0018640375 scopus 로고
    • Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin
    • Mowery, P. C., R. H. Lozier, Q. Chae, Y.-W. Tseng, M. Taylor, and W. Stoeckenius. 1979. Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin. Biochemistry. 18:4100-4107.
    • (1979) Biochemistry , vol.18 , pp. 4100-4107
    • Mowery, P.C.1    Lozier, R.H.2    Chae, Q.3    Tseng, Y.-W.4    Taylor, M.5    Stoeckenius, W.6
  • 30
    • 0026623260 scopus 로고
    • A unifying concept for ion translocation by retinal proteins
    • Oesterhelt, D., J. Tittor, and E. Bamberg. 1992. A unifying concept for ion translocation by retinal proteins. J. Bioenerg. Biomembr. 24:181-191.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 181-191
    • Oesterhelt, D.1    Tittor, J.2    Bamberg, E.3
  • 31
    • 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
    • Otto, H., T. Marti, M. Holz, T. Mogi, L. J. Stern, F. Engle, H. G. Khorana, and M. P. Heyn. 1990. 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. 87:1018-1022.
    • (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    Engle, F.6    Khorana, H.G.7    Heyn, M.P.8
  • 32
    • 0343880881 scopus 로고    scopus 로고
    • Guanidinium restores the purple chromophore of bacteriorhodopsin in the R82Q mutant
    • Renthal, R., and Y. J. Chung. 1996. Guanidinium restores the purple chromophore of bacteriorhodopsin in the R82Q mutant. Biophys. J. 70:A109.
    • (1996) Biophys. J. , vol.70
    • Renthal, R.1    Chung, Y.J.2
  • 33
    • 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. 35:4054-4062.
    • (1996) Biochemistry , vol.35 , pp. 4054-4062
    • Richter, H.-T.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 34
    • 0026643216 scopus 로고
    • FTIR difference spectroscopy of bacteriorhodopsin: Toward a molecular model
    • Rothschild, K. J. 1992. FTIR difference spectroscopy of bacteriorhodopsin: toward a molecular model. J. Bioenerg. Biomembr. 24:147-167.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 147-167
    • Rothschild, K.J.1
  • 35
    • 0029040316 scopus 로고    scopus 로고
    • Chemical reconstitution of a chloride pump inactivated by a single point mutation
    • Rüdiger, M., U. Haupts, K. Gerwert, and D. Oesterhelt. 1996. Chemical reconstitution of a chloride pump inactivated by a single point mutation. EMBO J. 14:1599-1606.
    • (1996) EMBO J. , vol.14 , pp. 1599-1606
    • Rüdiger, M.1    Haupts, U.2    Gerwert, K.3    Oesterhelt, D.4
  • 36
    • 0028218956 scopus 로고
    • Environmental effects on the protonation states of active site residues in bacteriorhodopsin
    • Sampogna, R. V., and B. Honig. 1994. Environmental effects on the protonation states of active site residues in bacteriorhodopsin. Biophys. J. 66:1341-1352.
    • (1994) Biophys. J. , vol.66 , pp. 1341-1352
    • Sampogna, R.V.1    Honig, B.2
  • 37
    • 0029781697 scopus 로고    scopus 로고
    • Electrostatic coupling between retinal isomerization and the ionization state of Glu-204: A general mechanism for proton release in bacteriorhodopsin
    • Sampogna, R. V., and B. Honig. 1996. Electrostatic coupling between retinal isomerization and the ionization state of Glu-204: a general mechanism for proton release in bacteriorhodopsin. Biophys. J. 71: 1165-1171.
    • (1996) Biophys. J. , vol.71 , pp. 1165-1171
    • Sampogna, R.V.1    Honig, B.2
  • 38
    • 84987064337 scopus 로고
    • Proton release pathway in bacteriorhodopsin: Molecular dynamics and electrostatic calculations
    • Scharnagl, C., J. Hettenkofer, and S. F. Fischer. 1994. Proton release pathway in bacteriorhodopsin: molecular dynamics and electrostatic calculations. Int. J. Quantum Chem. 521:33-56.
    • (1994) Int. J. Quantum Chem. , vol.521 , pp. 33-56
    • Scharnagl, C.1    Hettenkofer, J.2    Fischer, S.F.3
  • 39
    • 0000038837 scopus 로고
    • Electrostatic and conformational effects on the proton translocation steps in bacteriorhodopsin: Analysis of multiple M structures
    • Scharnagl, C., J. Hettenkofer, and S. F. Fischer. 1995. Electrostatic and conformational effects on the proton translocation steps in bacteriorhodopsin: analysis of multiple M structures. J. Phys. Chem 99:7787-7800.
    • (1995) J. Phys. Chem , vol.99 , pp. 7787-7800
    • Scharnagl, C.1    Hettenkofer, J.2    Fischer, S.F.3
  • 40
    • 0006300370 scopus 로고
    • Proton movement and surface charge in bacteriorhodopsin detected by selectively attached pH indicators
    • J. L. Rigaud, editor. John Libbey Eurotext, Montrouge, France
    • Scherrer, P., U. Alexiev, H. Otto, M. P. Heyn, T. Marti, and H. G. Khorana. 1992. Proton movement and surface charge in bacteriorhodopsin detected by selectively attached pH indicators. In Structures and Functions of Retinal Proteins. J. L. Rigaud, editor. John Libbey Eurotext, Montrouge, France. 205-211.
    • (1992) Structures and Functions of Retinal Proteins , pp. 205-211
    • Scherrer, P.1    Alexiev, U.2    Otto, H.3    Heyn, M.P.4    Marti, T.5    Khorana, H.G.6
  • 41
    • 25344464899 scopus 로고
    • Chemical modification of bacteriorhodopsin by fluorescamine
    • Singh, A. K., and S. M. Sonar. 1988. Chemical modification of bacteriorhodopsin by fluorescamine. Biochim. Biophys. Acta. 955:261-268.
    • (1988) Biochim. Biophys. Acta , vol.955 , pp. 261-268
    • Singh, A.K.1    Sonar, S.M.2
  • 42
    • 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
    • Subramaniam, S., T. Marti, and H. G. Khorana. 1990. 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. 87:1013-1017.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1013-1017
    • Subramaniam, S.1    Marti, T.2    Khorana, H.G.3
  • 43
    • 0024849644 scopus 로고
    • Isolation of a gene that encodes a new retinal protein, archaerhodopsin, from Halobacterium sp. aus-1
    • Sugiyama, Y., M. Maeda, M. Futai, and Y. Mukohata. 1989. Isolation of a gene that encodes a new retinal protein, archaerhodopsin, from Halobacterium sp. aus-1. J. Biol. Chem. 264:20859-20862.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20859-20862
    • Sugiyama, Y.1    Maeda, M.2    Futai, M.3    Mukohata, Y.4
  • 44
    • 84985447448 scopus 로고
    • Light-induced proton dissociation and association in bacteriorhodopsin
    • Takeuchi, Y., K. Ohno, M. Yoshida, and K. Nagano. 1981. Light-induced proton dissociation and association in bacteriorhodopsin. Photochem. Photobiol. 37:587-592.
    • (1981) Photochem. Photobiol. , vol.37 , pp. 587-592
    • Takeuchi, Y.1    Ohno, K.2    Yoshida, M.3    Nagano, K.4
  • 45
    • 0025856631 scopus 로고
    • Archaerhodopsin-2. from Halobacterium sp. aus-2 further reveals essential amino acid residues for light-driven proton pumps
    • Uegaki, K., Y. Sugiyama, and Mukohata. 1991. Archaerhodopsin-2. from Halobacterium sp. aus-2 further reveals essential amino acid residues for light-driven proton pumps. Arch. Biochem. Biophys. 286:107-110.
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 107-110
    • Uegaki, K.1    Sugiyama, Y.2    Mukohata3


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