메뉴 건너뛰기




Volumn 1607, Issue 1, 2003, Pages 19-26

Identification of intramembrane hydrogen bonding between 131 keto group of bacteriochlorophyll and serine residue α27 in the LH2 light-harvesting complex

Author keywords

Antenna complex; Chlorophyll binding pocket; Heat denaturation; Intramembrane H bonding; Photosystem I; Raman resonance spectroscopy

Indexed keywords

ALANINE; BACTERIAL PROTEIN; BACTERIOCHLOROPHYLL; CARBONYL DERIVATIVE; HISTIDINE; HYDROGEN; IMIDAZOLE; METHYL GROUP; MUTANT PROTEIN; POLYPEPTIDE; SERINE;

EID: 0141594870     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.08.004     Document Type: Article
Times cited : (17)

References (51)
  • 1
    • 0035367173 scopus 로고    scopus 로고
    • Helical membrane proteins: Diversity of functions in the context of simple architecture
    • Ubarretxena-Belandia I., Engelman D.M. Helical membrane proteins: diversity of functions in the context of simple architecture. Curr. Opin. Struct. Biol. 11:2001;370-376.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 370-376
    • Ubarretxena-Belandia, I.1    Engelman, D.M.2
  • 4
    • 0028388549 scopus 로고
    • Chlorophyll regulates accumulation of the plastid-encoded chlorophyll proteins P700 and D1 by increasing apoprotein stability
    • Kim J., Eichacker L.A., Rudiger W., Mullet J.E. Chlorophyll regulates accumulation of the plastid-encoded chlorophyll proteins P700 and D1 by increasing apoprotein stability. Plant Physiol. 104:1994;907-916.
    • (1994) Plant Physiol. , vol.104 , pp. 907-916
    • Kim, J.1    Eichacker, L.A.2    Rudiger, W.3    Mullet, J.E.4
  • 5
    • 0028872256 scopus 로고
    • Light-harvesting chlorophyll a/b complexes: Interdependent pigment synthesis and protein assembly
    • Plumley G.F., Schmidt G.W. Light-harvesting chlorophyll a/b complexes: interdependent pigment synthesis and protein assembly. Plant Cell. 7:1995;689-704.
    • (1995) Plant Cell , vol.7 , pp. 689-704
    • Plumley, G.F.1    Schmidt, G.W.2
  • 6
    • 0028927242 scopus 로고
    • Reconstitution of the bacterial core light-harvesting complexes of Rhodobacter sphaeroides and Rhodospirillum rubrum with isolated alpha- and beta-polypeptides, bacteriochlorophyll alpha, and carotenoid
    • Davis C.M., Bustamante P.L., Loach P.A. Reconstitution of the bacterial core light-harvesting complexes of Rhodobacter sphaeroides and Rhodospirillum rubrum with isolated alpha- and beta-polypeptides, bacteriochlorophyll alpha, and carotenoid. J. Biol. Chem. 270:1995;5793-5804.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5793-5804
    • Davis, C.M.1    Bustamante, P.L.2    Loach, P.A.3
  • 7
    • 0036301968 scopus 로고    scopus 로고
    • Folding in vitro of light-harvesting chlorophyll a/b protein is coupled with pigment binding
    • Horn R., Paulsen H. Folding in vitro of light-harvesting chlorophyll a/b protein is coupled with pigment binding. J. Mol. Biol. 318:2002;547-556.
    • (2002) J. Mol. Biol. , vol.318 , pp. 547-556
    • Horn, R.1    Paulsen, H.2
  • 9
    • 0033584940 scopus 로고    scopus 로고
    • Chlorophyll binding to monomeric light-harvesting complex. A mutation analysis of chromophore-binding residues
    • Remelli R., Varotto C., Sandona D., Croce R., Bassi R. Chlorophyll binding to monomeric light-harvesting complex. A mutation analysis of chromophore-binding residues. J. Biol. Chem. 274:1999;33510-33521.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33510-33521
    • Remelli, R.1    Varotto, C.2    Sandona, D.3    Croce, R.4    Bassi, R.5
  • 10
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan P., Fromme P., Witt H.T., Klukas O., Saenger W., Krauss N. Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature. 411:2001;909-917.
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 11
    • 0000455514 scopus 로고
    • Bacterial reaction centers with modified tetrapyrrol chromophores
    • R. Blankenship, M.T. Madigan, & C.E. Bauer. Dordrecht: Kluwer Academic Publishers
    • Scheer H., Hartwich G. Bacterial reaction centers with modified tetrapyrrol chromophores. Blankenship R., Madigan M.T., Bauer C.E. Anoxygenic Photosynthetic Bacteria. 1995;649-663 Kluwer Academic Publishers, Dordrecht.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 649-663
    • Scheer, H.1    Hartwich, G.2
  • 12
    • 0031805294 scopus 로고    scopus 로고
    • Reconstitution of the B800 bacteriochlorophylls in the peripheral light harvesting complex B800-850 of Rhodobacter sphaeroides 2.4.1 with BChl a and modified (bacterio)chlorophyll
    • Bandilla M., Ucker B., Ram M., Simonin I., Gelhaye E., McDermott G., Cogdell R.J., Scheer H. Reconstitution of the B800 bacteriochlorophylls in the peripheral light harvesting complex B800-850 of Rhodobacter sphaeroides 2.4.1 with BChl a and modified (bacterio)chlorophyll. Biochim. Biophys. Acta. 1364:1998;390-402.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 390-402
    • Bandilla, M.1    Ucker, B.2    Ram, M.3    Simonin, I.4    Gelhaye, E.5    McDermott, G.6    Cogdell, R.J.7    Scheer, H.8
  • 13
    • 0028216091 scopus 로고
    • Blue shifts in bacteriochlorophyll absorbance correlate with changed hydrogen bonding patterns in light-harvesting 2 mutants of Rhodobacter sphaeroides with alterations at alpha-Tyr-44 and alpha-Tyr-45
    • Fowler G.J., Sockalingum G.D., Robert B., Hunter C.N. Blue shifts in bacteriochlorophyll absorbance correlate with changed hydrogen bonding patterns in light-harvesting 2 mutants of Rhodobacter sphaeroides with alterations at alpha-Tyr-44 and alpha-Tyr-45. Biochem. J. 299:1994;695-700.
    • (1994) Biochem. J. , vol.299 , pp. 695-700
    • Fowler, G.J.1    Sockalingum, G.D.2    Robert, B.3    Hunter, C.N.4
  • 14
    • 0031234813 scopus 로고    scopus 로고
    • Pigment binding site and electronic properties in light-harvesting proteins of purple bacteria
    • Sturgis J.N., Robert B. Pigment binding site and electronic properties in light-harvesting proteins of purple bacteria. J. Phys. Chem. 101:1997;7227-7231.
    • (1997) J. Phys. Chem. , vol.101 , pp. 7227-7231
    • Sturgis, J.N.1    Robert, B.2
  • 15
    • 0037063333 scopus 로고    scopus 로고
    • Tuning of the redox potential of the primary electron donor in reaction centres of purple bacteria: Effects of amino acid polarity and position
    • Spiedel D., Jones M.R., Robert B. Tuning of the redox potential of the primary electron donor in reaction centres of purple bacteria: effects of amino acid polarity and position. FEBS Lett. 527:2002;171-175.
    • (2002) FEBS Lett. , vol.527 , pp. 171-175
    • Spiedel, D.1    Jones, M.R.2    Robert, B.3
  • 16
    • 0032566323 scopus 로고    scopus 로고
    • Effects of hydrogen bonds on the redox potential and electronic structure of the bacterial primary electron donor
    • Ivancich A., Artz K., Williams J.C., Allen J.P., Mattioli T.A. Effects of hydrogen bonds on the redox potential and electronic structure of the bacterial primary electron donor. Biochemistry. 37:1998;11812-11820.
    • (1998) Biochemistry , vol.37 , pp. 11812-11820
    • Ivancich, A.1    Artz, K.2    Williams, J.C.3    Allen, J.P.4    Mattioli, T.A.5
  • 17
    • 0028338712 scopus 로고
    • Modification of a hydrogen bond to a bacteriochlorophyll a molecule in the light-harvesting 1 antenna of Rhodobacter sphaeroides
    • Olsen J.D., Sockalingum G.D., Robert B., Hunter C.N. Modification of a hydrogen bond to a bacteriochlorophyll a molecule in the light-harvesting 1 antenna of Rhodobacter sphaeroides. Proc. Natl. Acad. Sci. U. S. A. 91:1994;7124-7128.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 7124-7128
    • Olsen, J.D.1    Sockalingum, G.D.2    Robert, B.3    Hunter, C.N.4
  • 18
    • 0001886554 scopus 로고    scopus 로고
    • Application of resonance Raman spectroscopy in photosynthesis
    • Amsterdam: Kluwer Academic Publisher
    • Robert B. Application of resonance Raman spectroscopy in photosynthesis. Biophysical Techniques in Photosynthesis. 1996;161-176 Kluwer Academic Publisher, Amsterdam.
    • (1996) Biophysical Techniques in Photosynthesis , pp. 161-176
    • Robert, B.1
  • 20
    • 0030862122 scopus 로고    scopus 로고
    • Site-directed modification of the ligands to the bacteriochlorophylls of the light-harvesting LH1 and LH2 complexes of Rhodobacter sphaeroides
    • Olsen J.D., Sturgis J.N., Westerhuis W.H., Fowler G.J., Hunter C.N., Robert B. Site-directed modification of the ligands to the bacteriochlorophylls of the light-harvesting LH1 and LH2 complexes of Rhodobacter sphaeroides. Biochemistry. 36:1997;12625-12632.
    • (1997) Biochemistry , vol.36 , pp. 12625-12632
    • Olsen, J.D.1    Sturgis, J.N.2    Westerhuis, W.H.3    Fowler, G.J.4    Hunter, C.N.5    Robert, B.6
  • 21
    • 0032214447 scopus 로고    scopus 로고
    • Heterologous expression of genes encoding bacterial light-harvesting complex II in Rhodobacter capsulatus and Rhodovulum sulfidophilum
    • Katsiou E., Sturgis J.N., Robert B., Tadros M.H. Heterologous expression of genes encoding bacterial light-harvesting complex II in Rhodobacter capsulatus and Rhodovulum sulfidophilum. Microbiol. Res. 153:1998;189-204.
    • (1998) Microbiol. Res. , vol.153 , pp. 189-204
    • Katsiou, E.1    Sturgis, J.N.2    Robert, B.3    Tadros, M.H.4
  • 22
    • 0036042152 scopus 로고    scopus 로고
    • Assembly of light-harvesting bacteriochlorophyll in a model transmembrane helix in its natural environment
    • Braun P., Olsen J., Strohmann B., Hunter C.N., Scheer H. Assembly of light-harvesting bacteriochlorophyll in a model transmembrane helix in its natural environment. J. Mol. Biol. 318:2002;1085-1095.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1085-1095
    • Braun, P.1    Olsen, J.2    Strohmann, B.3    Hunter, C.N.4    Scheer, H.5
  • 23
    • 0028917697 scopus 로고
    • Structure and properties of the bacteriochlorophyll binding site in peripheral light-harvesting complexes of purple bacteria
    • Sturgis J.N., Jirsakova V., Reiss-Husson F., Cogdell R.J., Robert B. Structure and properties of the bacteriochlorophyll binding site in peripheral light-harvesting complexes of purple bacteria. Biochemistry. 34:1995;517-523.
    • (1995) Biochemistry , vol.34 , pp. 517-523
    • Sturgis, J.N.1    Jirsakova, V.2    Reiss-Husson, F.3    Cogdell, R.J.4    Robert, B.5
  • 24
    • 0026586530 scopus 로고
    • Mutants of Rhodobacter sphaeroides lacking one or more pigment-protein complexes and complementation with reaction-centre, LH1, and LH2 genes
    • Jones M.R., Fowler G.J., Gibson L.C., Grief G.G., Olsen J.D., Crielaard W., Hunter C.N. Mutants of Rhodobacter sphaeroides lacking one or more pigment-protein complexes and complementation with reaction-centre, LH1, and LH2 genes. Mol. Microbiol. 6:1992;1173-1184.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1173-1184
    • Jones, M.R.1    Fowler, G.J.2    Gibson, L.C.3    Grief, G.G.4    Olsen, J.D.5    Crielaard, W.6    Hunter, C.N.7
  • 28
    • 0031415406 scopus 로고    scopus 로고
    • Influence of the protein binding site on the absorption properties of the monomeric bacteriochlorophyll in Rhodobacter sphaeroides LH2 complex
    • Gall A., Fowler G.J., Hunter C.N., Robert B. Influence of the protein binding site on the absorption properties of the monomeric bacteriochlorophyll in Rhodobacter sphaeroides LH2 complex. Biochemistry. 36:1997;16282-16287.
    • (1997) Biochemistry , vol.36 , pp. 16282-16287
    • Gall, A.1    Fowler, G.J.2    Hunter, C.N.3    Robert, B.4
  • 29
    • 0021949019 scopus 로고
    • Structures of antenna complexes of several Rhodospirillales from their resonance Raman spectra
    • Robert B., Lutz M. Structures of antenna complexes of several Rhodospirillales from their resonance Raman spectra. Biochim. Biophys. Acta. 807:1985;10-23.
    • (1985) Biochim. Biophys. Acta , vol.807 , pp. 10-23
    • Robert, B.1    Lutz, M.2
  • 30
    • 0038131017 scopus 로고    scopus 로고
    • Influence of carotenoid molecules on the structure of the bacteriochlorophyll binding site in peripheral light-harvesting proteins from Rhodobacter sphaeroides
    • Gall A., Cogdell R., Robert B. Influence of carotenoid molecules on the structure of the bacteriochlorophyll binding site in peripheral light-harvesting proteins from Rhodobacter sphaeroides. Biochemistry. 42:2003;7252-7258.
    • (2003) Biochemistry , vol.42 , pp. 7252-7258
    • Gall, A.1    Cogdell, R.2    Robert, B.3
  • 31
    • 0036296028 scopus 로고    scopus 로고
    • Twist and shear in beta-sheets and beta-ribbons
    • Ho B., Curmi P.M. Twist and shear in beta-sheets and beta-ribbons. J. Mol. Biol. 317:2003;291-308.
    • (2003) J. Mol. Biol. , vol.317 , pp. 291-308
    • Ho, B.1    Curmi, P.M.2
  • 33
    • 0035984036 scopus 로고    scopus 로고
    • Hydrogen bridges in crystal engineering: Interactions without borders
    • Desiraju G.R. Hydrogen bridges in crystal engineering: interactions without borders. Acc. Chem. Res. 35:2002;565-573.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 565-573
    • Desiraju, G.R.1
  • 34
    • 0037019829 scopus 로고    scopus 로고
    • CH...O hydrogen bonds at protein-protein interfaces
    • Jiang L., Lai L. CH...O hydrogen bonds at protein-protein interfaces. J. Biol. Chem. 277:2002;37732-37740.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37732-37740
    • Jiang, L.1    Lai, L.2
  • 35
    • 0000539541 scopus 로고
    • Hydrogen bond energies and band shifts of the stretching vibrations of C:O groups
    • Zadorozhnyi B., Ishchenko I. Hydrogen bond energies and band shifts of the stretching vibrations of C:O groups. Opt. Spectrosc. 19:1965;306-308.
    • (1965) Opt. Spectrosc. , vol.19 , pp. 306-308
    • Zadorozhnyi, B.1    Ishchenko, I.2
  • 36
    • 0029810225 scopus 로고    scopus 로고
    • Pigment-protein interactions in the antenna-reaction center complex of Heliobacillus mobilis
    • Liebl U., Nitschke W.A., Mattioli T.A. Pigment-protein interactions in the antenna-reaction center complex of Heliobacillus mobilis. Photochem. Photobiol. 64:1996;38-45.
    • (1996) Photochem. Photobiol. , vol.64 , pp. 38-45
    • Liebl, U.1    Nitschke, W.A.2    Mattioli, T.A.3
  • 37
    • 0025292375 scopus 로고
    • Structure of the primary electron donor in photosystem I: A resonance Raman study
    • Moenne-Loccoz P., Robert B., Ikegami I., Lutz M. Structure of the primary electron donor in photosystem I: a resonance Raman study. Biochemistry. 29:1990;4740-4746.
    • (1990) Biochemistry , vol.29 , pp. 4740-4746
    • Moenne-Loccoz, P.1    Robert, B.2    Ikegami, I.3    Lutz, M.4
  • 39
    • 0025907860 scopus 로고
    • Resonance Raman characterization of Rhodobacter sphaeroides reaction centers bearing site-directed mutations at Tyrosine M210
    • Mattioli T.A., Gray K.A., Lutz M., Oesterhelt D., Robert B. Resonance Raman characterization of Rhodobacter sphaeroides reaction centers bearing site-directed mutations at Tyrosine M210. Biochemistry. 30:1991;1715-1721.
    • (1991) Biochemistry , vol.30 , pp. 1715-1721
    • Mattioli, T.A.1    Gray, K.A.2    Lutz, M.3    Oesterhelt, D.4    Robert, B.5
  • 40
    • 0035812387 scopus 로고    scopus 로고
    • Modeling the bacterial photosynthetic reaction center: 4. The structural, electrochemical, and hydrogen-bonding properties of 22 mutants of Rhodobacter sphaeroides
    • Hughes J.M., Hutter M.C., Reimers J.R., Hush N.S. Modeling the bacterial photosynthetic reaction center: 4. The structural, electrochemical, and hydrogen-bonding properties of 22 mutants of Rhodobacter sphaeroides. J. Am. Chem. Soc. 123:2001;8550-8563.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8550-8563
    • Hughes, J.M.1    Hutter, M.C.2    Reimers, J.R.3    Hush, N.S.4
  • 41
    • 0030940620 scopus 로고    scopus 로고
    • Functions of conserved tryptophan residues of the core light-harvesting complex of Rhodobacter sphaeroides
    • Sturgis J.N., Olsen J.D., Robert B., Hunter C.N. Functions of conserved tryptophan residues of the core light-harvesting complex of Rhodobacter sphaeroides. Biochemistry. 36:1997;2772-2778.
    • (1997) Biochemistry , vol.36 , pp. 2772-2778
    • Sturgis, J.N.1    Olsen, J.D.2    Robert, B.3    Hunter, C.N.4
  • 42
    • 33751553603 scopus 로고
    • Conformational and environmental effects on bacteriochlorophyll optical spectra: Correlations of calculated spectra with structural results
    • Gudowska-Nowak E., Newton M.D., Fajer J. Conformational and environmental effects on bacteriochlorophyll optical spectra: correlations of calculated spectra with structural results. J. Phys Chem. 94:1990;5795-5801.
    • (1990) J. Phys Chem. , vol.94 , pp. 5795-5801
    • Gudowska-Nowak, E.1    Newton, M.D.2    Fajer, J.3
  • 43
    • 0035909103 scopus 로고    scopus 로고
    • Thermal destabilization of rhodopsin and opsin by proteolytic cleavage in bovine rod outer segment disk membranes
    • Landin J.S., Katragadda M., Albert A.D. Thermal destabilization of rhodopsin and opsin by proteolytic cleavage in bovine rod outer segment disk membranes. Biochemistry. 40:2001;11176-11183.
    • (2001) Biochemistry , vol.40 , pp. 11176-11183
    • Landin, J.S.1    Katragadda, M.2    Albert, A.D.3
  • 44
    • 0042216240 scopus 로고
    • Thermal denaturation of photosynthetic membrane proteins from Rhodobacter sphaeroides
    • Ishimura M., Honda S., Uedaira H., Odahara T., Miyake J. Thermal denaturation of photosynthetic membrane proteins from Rhodobacter sphaeroides. Thermochim. Acta. 266:1995;355-364.
    • (1995) Thermochim. Acta , vol.266 , pp. 355-364
    • Ishimura, M.1    Honda, S.2    Uedaira, H.3    Odahara, T.4    Miyake, J.5
  • 45
    • 0028954453 scopus 로고
    • Temperature-induced micellar-lamellar transformation in binary mixtures of saturated phosphatidylcholines with sodium cholate
    • Polozova A.I., Dubachev G.E., Simonova T.N., Barsukov L.I. Temperature-induced micellar-lamellar transformation in binary mixtures of saturated phosphatidylcholines with sodium cholate. FEBS Lett. 358:1995;17-22.
    • (1995) FEBS Lett. , vol.358 , pp. 17-22
    • Polozova, A.I.1    Dubachev, G.E.2    Simonova, T.N.3    Barsukov, L.I.4
  • 46
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions
    • Senes A., Gerstein M., Engelman D.M. Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions. J. Mol. Biol. 296:2000;921-936.
    • (2000) J. Mol. Biol. , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 48
    • 0035969998 scopus 로고    scopus 로고
    • Polar side chains drive the association of model transmembrane peptides
    • Gratkowski H., Lear J.D., DeGrado W.F. Polar side chains drive the association of model transmembrane peptides. Proc. Natl. Acad. Sci. U. S. A. 98:2001;880-885.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 880-885
    • Gratkowski, H.1    Lear, J.D.2    DeGrado, W.F.3
  • 50
    • 0035979146 scopus 로고    scopus 로고
    • The Cα-H...O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions
    • Senes A., Ubarretxena-Belandia I., Engelman D.M. The Cα-H...O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions. Proc. Natl. Acad. Sci. U. S. A. 98:2001;9056-9061.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9056-9061
    • Senes, A.1    Ubarretxena-Belandia, I.2    Engelman, D.M.3
  • 51
    • 0033747337 scopus 로고    scopus 로고
    • Serine and threonine residues bend alpha-helices in the chi(1)=g(-) conformation
    • Ballesteros J.A., Deupi X., Olivella M., Haaksma E.E., Pardo L. Serine and threonine residues bend alpha-helices in the chi(1)=g(-) conformation. Biophys. J. 79:2000;2754-2760.
    • (2000) Biophys. J. , vol.79 , pp. 2754-2760
    • Ballesteros, J.A.1    Deupi, X.2    Olivella, M.3    Haaksma, E.E.4    Pardo, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.