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Volumn 89, Issue 12, 2010, Pages 983-989

Histidine is involved in coupling proton uptake to electron transfer in photosynthetic proteins

Author keywords

Band assignment; Electron transfer; Fourier transform infrared; Histidine; Isotopic labeling; L210DN; Photosynthesis; Protonated water; Reaction center

Indexed keywords

AMINO ACID; HISTIDINE; IRON; PROTON;

EID: 78149409234     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2010.08.007     Document Type: Article
Times cited : (18)

References (33)
  • 1
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • Barth A. The infrared absorption of amino acid side chains. Prog. Biophys. Mol. Biol. 2000, 74:141-173.
    • (2000) Prog. Biophys. Mol. Biol. , vol.74 , pp. 141-173
    • Barth, A.1
  • 2
    • 0017184389 scopus 로고
    • A Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0029111537 scopus 로고
    • Binding sites of quinones in photosynthetic bacterial reaction centers investigated by light-induced FTIR difference spectroscopy: symmetry of the carbonyl interactions and close equivalence of the QB vibrations in Rhodobacter sphaeroides and Rhodopseudomonas viridis probed by isotope labeling
    • Breton J., Boullais C., Berger G., Mioskowski C., Nabedryk E. Binding sites of quinones in photosynthetic bacterial reaction centers investigated by light-induced FTIR difference spectroscopy: symmetry of the carbonyl interactions and close equivalence of the QB vibrations in Rhodobacter sphaeroides and Rhodopseudomonas viridis probed by isotope labeling. Biochemistry 1995, 34:11606-11616.
    • (1995) Biochemistry , vol.34 , pp. 11606-11616
    • Breton, J.1    Boullais, C.2    Berger, G.3    Mioskowski, C.4    Nabedryk, E.5
  • 4
    • 85083143758 scopus 로고    scopus 로고
    • Infrared vibrational modes of histidine ligands of the primary electron donor and of QA in purple photosynthetic bacteria
    • CSIRO Publishing, Collingwood, Victoria, Australia
    • Breton J., Richaud P., Verméglio A., Nabedryk E. Infrared vibrational modes of histidine ligands of the primary electron donor and of QA in purple photosynthetic bacteria. PS2001Proceedings of the 12th International Congress on Photosynthesis, S7-002 2001, CSIRO Publishing, Collingwood, Victoria, Australia.
    • (2001) PS2001Proceedings of the 12th International Congress on Photosynthesis, S7-002
    • Breton, J.1    Richaud, P.2    Verméglio, A.3    Nabedryk, E.4
  • 6
    • 0028281478 scopus 로고
    • Crystallographic analyses of site-directed mutants of the photosynthetic reaction center from Rhodobacter sphaeroides
    • Chirino A.J., Lous E.J., Huber M., Allen J.P., Schenck C.C., Paddock M.L., Feher G., Rees D.C. Crystallographic analyses of site-directed mutants of the photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry 1994, 33:4584-4593.
    • (1994) Biochemistry , vol.33 , pp. 4584-4593
    • Chirino, A.J.1    Lous, E.J.2    Huber, M.3    Allen, J.P.4    Schenck, C.C.5    Paddock, M.L.6    Feher, G.7    Rees, D.C.8
  • 7
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65Å resolution: cofactors and protein-cofactor interactions
    • Ermler U., Fritzsch G., Buchanan S.K., Michel H. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65Å resolution: cofactors and protein-cofactor interactions. Structure 1994, 2(10):925-936.
    • (1994) Structure , vol.2 , Issue.10 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 8
    • 0001864802 scopus 로고
    • A Rhodobacter sphaeroides puf L, M and X deletion mutant and its complementation in trans with a 5.3kb puf operon shuttle fragment
    • Farchaus J.W., Oesterhelt D. A Rhodobacter sphaeroides puf L, M and X deletion mutant and its complementation in trans with a 5.3kb puf operon shuttle fragment. EMBO J. 1989, 8(1):47-54.
    • (1989) EMBO J. , vol.8 , Issue.1 , pp. 47-54
    • Farchaus, J.W.1    Oesterhelt, D.2
  • 9
    • 0032578541 scopus 로고    scopus 로고
    • - in bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay
    • - in bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:11679-11684.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 11679-11684
    • Graige, M.S.1    Feher, G.2    Okamura, M.Y.3
  • 10
    • 0001617001 scopus 로고    scopus 로고
    • Vibrational spectra and ab initio DFT calculations of 4-methylimidazole and its different protonation forms: infrared and Raman markers of the protonation state of a histidine side chain
    • Hasegawa K., Ono T.-A., Noguchi T. Vibrational spectra and ab initio DFT calculations of 4-methylimidazole and its different protonation forms: infrared and Raman markers of the protonation state of a histidine side chain. J. Phys. Chem. 2000, 104:4253-4265.
    • (2000) J. Phys. Chem. , vol.104 , pp. 4253-4265
    • Hasegawa, K.1    Ono, T.-A.2    Noguchi, T.3
  • 12
    • 33751242792 scopus 로고    scopus 로고
    • Proton uptake in the reaction center mutant L210DN from Rhodobacter sphaeroides via protonated water molecules
    • Hermes S., Stachnik J.M., Onidas D., Remy A., Hofmann E., Gerwert K. Proton uptake in the reaction center mutant L210DN from Rhodobacter sphaeroides via protonated water molecules. Biochemistry 2006, 45:13741-13749.
    • (2006) Biochemistry , vol.45 , pp. 13741-13749
    • Hermes, S.1    Stachnik, J.M.2    Onidas, D.3    Remy, A.4    Hofmann, E.5    Gerwert, K.6
  • 13
    • 0027429642 scopus 로고
    • A modelindependent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates
    • Hessling B., Souvignier G., Gerwert K. A modelindependent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates. Biophys. J. 1993, 65:1929-1941.
    • (1993) Biophys. J. , vol.65 , pp. 1929-1941
    • Hessling, B.1    Souvignier, G.2    Gerwert, K.3
  • 17
    • 15544382668 scopus 로고    scopus 로고
    • Direct observation of redox-linked histidine protonation changes in the iron-sulfur protein of the cytochrome bc1 complex by ATR-FTIR spectroscopy
    • Iwaki M., Yakolev G., Hirst J., Osyczka A., Dutton P.L., Marshall D., Rich P.P. Direct observation of redox-linked histidine protonation changes in the iron-sulfur protein of the cytochrome bc1 complex by ATR-FTIR spectroscopy. Biochemistry 2005, 44:4230-4237.
    • (2005) Biochemistry , vol.44 , pp. 4230-4237
    • Iwaki, M.1    Yakolev, G.2    Hirst, J.3    Osyczka, A.4    Dutton, P.L.5    Marshall, D.6    Rich, P.P.7
  • 18
    • 34447282051 scopus 로고    scopus 로고
    • PH modulates the quinone position in the photosynthetic reaction center from Rhodobacter sphaeroides in the neutral and charge separated states
    • Koepke J., Krammer E.-M., Klingen A.R., Sebban P., Ullmann G.M., Fritzsch G. pH modulates the quinone position in the photosynthetic reaction center from Rhodobacter sphaeroides in the neutral and charge separated states. J. Mol. Biol. 2007, 371(2):396-409.
    • (2007) J. Mol. Biol. , vol.371 , Issue.2 , pp. 396-409
    • Koepke, J.1    Krammer, E.-M.2    Klingen, A.R.3    Sebban, P.4    Ullmann, G.M.5    Fritzsch, G.6
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227(5259):680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0032478280 scopus 로고    scopus 로고
    • - and the associated processes in Rhodobacter sphaeroides R-26 reaction centers
    • - and the associated processes in Rhodobacter sphaeroides R-26 reaction centers. Biochemistry 1998, 37:2818-2829.
    • (1998) Biochemistry , vol.37 , pp. 2818-2829
    • Li, J.1    Gilroy, D.2    Tiede, D.M.3    Gunner, M.R.4
  • 22
    • 0028973591 scopus 로고
    • Fourier transform infrared difference spectroscopy of secondary quinone acceptor photoreduction in proton transfer mutants of Rhodobacter sphaeroides
    • Nabedryk E., Breton J., Hienerwadel R., Fogel C., Mäntele W., Paddock M.L., Okamura M.Y. Fourier transform infrared difference spectroscopy of secondary quinone acceptor photoreduction in proton transfer mutants of Rhodobacter sphaeroides. Biochemistry 1995, 34:14722-14732.
    • (1995) Biochemistry , vol.34 , pp. 14722-14732
    • Nabedryk, E.1    Breton, J.2    Hienerwadel, R.3    Fogel, C.4    Mäntele, W.5    Paddock, M.L.6    Okamura, M.Y.7
  • 24
    • 0242657390 scopus 로고    scopus 로고
    • Proton transfer pathways and mechanism in bacterial reaction centers
    • Paddock M.L., Feher G., Okamura M.Y. Proton transfer pathways and mechanism in bacterial reaction centers. FEBS Lett. 2003, 555:45-50.
    • (2003) FEBS Lett. , vol.555 , pp. 45-50
    • Paddock, M.L.1    Feher, G.2    Okamura, M.Y.3
  • 25
    • 0025259038 scopus 로고
    • Mass spectrometric determination of isotopically labeled tyrosines and tryptophans in photosynthetic reaction centers of Rhodobacter sphaeroides R-26
    • Raap J., Winkel C., de Wit A.H., van Houten A.H., Hoff A.J., Lugtenburg J. Mass spectrometric determination of isotopically labeled tyrosines and tryptophans in photosynthetic reaction centers of Rhodobacter sphaeroides R-26. Anal. Biochem. 1990, 191(1):9-15.
    • (1990) Anal. Biochem. , vol.191 , Issue.1 , pp. 9-15
    • Raap, J.1    Winkel, C.2    de Wit, A.H.3    van Houten, A.H.4    Hoff, A.J.5    Lugtenburg, J.6
  • 26
    • 85083126713 scopus 로고    scopus 로고
    • Der QA-QB→QAQB- Übergang im bakteriellen photosynthetischen Reaktionszentrum von Rhodobacter sphaeroides (The QA-QB→QAQB- transition in the bacterial photosynthetic reaction centre of Rhodobacter sphaeroides). Thesis of Ruhr-University Bochum, Bochum, Ge
    • Remy, A., 2002. Der QA-QB→QAQB- Übergang im bakteriellen photosynthetischen Reaktionszentrum von Rhodobacter sphaeroides (The QA-QB→QAQB- transition in the bacterial photosynthetic reaction centre of Rhodobacter sphaeroides). Thesis of Ruhr-University Bochum, Bochum, Germany.
    • (2002)
    • Remy, A.1
  • 27
    • 0041622652 scopus 로고    scopus 로고
    • Coupling of light-induced electron transfer to proton uptake in photosynthesis
    • Remy A., Gerwert K. Coupling of light-induced electron transfer to proton uptake in photosynthesis. Nat. Struct. Biol. 2003, 10:637-644.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 637-644
    • Remy, A.1    Gerwert, K.2
  • 28
    • 0030904273 scopus 로고    scopus 로고
    • Light induced structural changes in photosynthetic reaction center: Implications for mechanism of electron-proton transfer
    • Stowell M.H.B., McPhillips T.M., Rees D.C., Soltis S.M., Abresch E., Feher G. Light induced structural changes in photosynthetic reaction center: Implications for mechanism of electron-proton transfer. Science 1997, 276:812-816.
    • (1997) Science , vol.276 , pp. 812-816
    • Stowell, M.H.B.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 29
    • 0029769668 scopus 로고    scopus 로고
    • Time-resolved electrochromism associated with the formation of quinone anions in the Rhodobacter sphaeroides R26 reaction center
    • Tiede D.M., Vazquez J., Cordova J., Marone P.A. Time-resolved electrochromism associated with the formation of quinone anions in the Rhodobacter sphaeroides R26 reaction center. Biochemistry 1996, 35:10763-10775.
    • (1996) Biochemistry , vol.35 , pp. 10763-10775
    • Tiede, D.M.1    Vazquez, J.2    Cordova, J.3    Marone, P.A.4
  • 30
    • 48849084900 scopus 로고    scopus 로고
    • Systematic approach to group-specific isotopic labeling of proteins for vibrational spectroscopy
    • Warscheid B., Brucker S., Kallenbach A., Meyer H.E., Gerwert K., Kötting C. Systematic approach to group-specific isotopic labeling of proteins for vibrational spectroscopy. Vib. Spectrosc. 2008, 48:28-36.
    • (2008) Vib. Spectrosc. , vol.48 , pp. 28-36
    • Warscheid, B.1    Brucker, S.2    Kallenbach, A.3    Meyer, H.E.4    Gerwert, K.5    Kötting, C.6
  • 31
    • 33744536180 scopus 로고    scopus 로고
    • Infrared spectra and molar absorption coefficients of the 20 alpha amino acids in aqueous solutions in the spectral range from 1800 to 500cm(-1)
    • Wolpert M., Hellwig P. Infrared spectra and molar absorption coefficients of the 20 alpha amino acids in aqueous solutions in the spectral range from 1800 to 500cm(-1). Spectrochim. Acta A Mol. Biomol. Spectrosc. 2006, 64(4):987-1001.
    • (2006) Spectrochim. Acta A Mol. Biomol. Spectrosc. , vol.64 , Issue.4 , pp. 987-1001
    • Wolpert, M.1    Hellwig, P.2
  • 32
    • 1242347393 scopus 로고    scopus 로고
    • Proton and electron transfer in the acceptor quinone complex of photosynthetic reaction centers from Rhodobacter spaeroides
    • Wraight C.A. Proton and electron transfer in the acceptor quinone complex of photosynthetic reaction centers from Rhodobacter spaeroides. Front. Biosci. 2004, 9:309-337.
    • (2004) Front. Biosci. , vol.9 , pp. 309-337
    • Wraight, C.A.1
  • 33
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8Å resolution
    • Zouni A., Witt H.T., Kern J., Fromme P., Krauss N., Saenger W., Orth P. Crystal structure of photosystem II from Synechococcus elongatus at 3.8Å resolution. Nature 2001, 409:739-743.
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7


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