메뉴 건너뛰기




Volumn 90, Issue 11, 2006, Pages 4155-4166

Kinetic analysis of the thermal stability of the photosynthetic reaction center from Rhodobacter sphaeroides

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOCHLORIN; BACTERIOCHLOROPHYLL; BACTERIOPHEOPHYTIN; POLYPEPTIDE;

EID: 33744911339     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.070029     Document Type: Article
Times cited : (36)

References (39)
  • 1
    • 0034855858 scopus 로고    scopus 로고
    • Review: How do thermophilic proteins deal with heat?
    • Kumar, S., and R. Nussinov. 2001. Review: How do thermophilic proteins deal with heat? Cell. Mol. Life Sci. 58:1216-1233.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1216-1233
    • Kumar, S.1    Nussinov, R.2
  • 2
    • 0041649675 scopus 로고    scopus 로고
    • Thermal denaturing of bacteriorhodopsin by x-ray scattering from oriented purple membranes
    • Müller, J., C. Münster, and T. Salditt. 2000. Thermal denaturing of bacteriorhodopsin by x-ray scattering from oriented purple membranes. Biophys. J. 78:3208-3217.
    • (2000) Biophys. J. , vol.78 , pp. 3208-3217
    • Müller, J.1    Münster, C.2    Salditt, T.3
  • 4
    • 0029112313 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • Haltia, T., and E. Friere. 1995. Forces and factors that contribute to the structural stability of membrane proteins. Biochim. Biophys. Acta. 1241:295-322.
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 295-322
    • Haltia, T.1    Friere, E.2
  • 5
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot, J. L., and D. M. Engelman. 1990. Membrane protein folding and oligomerization: the two-stage model. Biochemistry. 29:4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 6
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability. Physical principles
    • White, S. H., and W. C. Wimley. 1999. Membrane protein folding and stability. Physical principles. Annu. Rev. Biophys. Biomol. Struct. 28:319-365.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 7
    • 0034610266 scopus 로고    scopus 로고
    • Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: Thermostability and electron transfer
    • Nogi, T., I. Fathir, M. Kobayashi, T. Nozawa, and K. Miki. 2000. Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer. Proc. Natl. Acad. Sci. USA. 97:13561-13566.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13561-13566
    • Nogi, T.1    Fathir, I.2    Kobayashi, M.3    Nozawa, T.4    Miki, K.5
  • 8
    • 0023395661 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26 - The cofactors
    • Allen, J. P., G. Feher, T. O. Yeates, H. Komia, and D. C. Rees. 1987. Structure of the reaction center from Rhodobacter sphaeroides R-26 - the cofactors. Proc. Natl. Acad. Sci. USA. 84:5730-5734.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5730-5734
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komia, H.4    Rees, D.C.5
  • 9
    • 0025784505 scopus 로고
    • Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides
    • Chang, C. H., O. El Kabbani, D. Tiede, J. Norris, and M. Schiffer. 1991. Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry. 30:5352-5360.
    • (1991) Biochemistry , vol.30 , pp. 5352-5360
    • Chang, C.H.1    El Kabbani, O.2    Tiede, D.3    Norris, J.4    Schiffer, M.5
  • 10
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction center from Rhodobacter sphaeroides at 2.65 Å resolution - Cofactors and protein-cofactor interactions
    • Ermler, U., G. Fritzsch, S. K. Buchanan, and H. Michel. 1994. Structure of the photosynthetic reaction center from Rhodobacter sphaeroides at 2.65 Å resolution - cofactors and protein-cofactor interactions. Structure. 2:925-936.
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 11
    • 0028210159 scopus 로고
    • Structure and function of the photosynthetic reaction center from Rhodobacter sphaeroides
    • Ermler, U., H. Michel, and M. Schiffer. 1994. Structure and function of the photosynthetic reaction center from Rhodobacter sphaeroides. J. Bioenerg. Biomembr. 26:5-15.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 5-15
    • Ermler, U.1    Michel, H.2    Schiffer, M.3
  • 12
    • 0021755973 scopus 로고
    • X-ray structure analysis of a membrane protein complex - Electron-density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis
    • Deisenhofer, J., O. Epp, K. Miki, R. Huber, and H. Michel. 1984. X-ray structure analysis of a membrane protein complex - electron-density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 180:385-398.
    • (1984) J. Mol. Biol. , vol.180 , pp. 385-398
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 13
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution
    • Deisenhofer, J., O. Epp, K. Miki, R. Huber, and H. Michel. 1985. Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution. Nature. 318:618-624.
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 14
    • 0028957690 scopus 로고
    • Crystallographic refinement at 2.3-Å resolution and refined model of the photosynthetic reaction center from Rhodopseudomonas viridis
    • Deisenhofer, J., O. Epp, I. Sinning, and H. Michel. 1995. Crystallographic refinement at 2.3-Å resolution and refined model of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 246:429-457.
    • (1995) J. Mol. Biol. , vol.246 , pp. 429-457
    • Deisenhofer, J.1    Epp, O.2    Sinning, I.3    Michel, H.4
  • 15
    • 25444501222 scopus 로고    scopus 로고
    • On the role of basic residues in adapting the reaction center-LH1 photosystem for growth at elevated temperatures in purple bacteria
    • In press
    • Watson, A. J., A. V. Hughes, P. K. Fyfe, M. C. Wakeham, P. Heathcote, and M. R. Jones. 2005. On the role of basic residues in adapting the reaction center-LH1 photosystem for growth at elevated temperatures in purple bacteria. Photosynth. Res. In press.
    • (2005) Photosynth. Res.
    • Watson, A.J.1    Hughes, A.V.2    Fyfe, P.K.3    Wakeham, M.C.4    Heathcote, P.5    Jones, M.R.6
  • 16
    • 0024971435 scopus 로고
    • Purification and characterization of the thermostable ribulose-1,5-bisphosphate carboxylase oxygenase from the thermophilic purple bacterium Chromatium tepidum
    • Heda, G., and M. Madigan. 1989. Purification and characterization of the thermostable ribulose-1,5-bisphosphate carboxylase oxygenase from the thermophilic purple bacterium Chromatium tepidum. Eur. J. Biochem. 184:313-319.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 313-319
    • Heda, G.1    Madigan, M.2
  • 17
    • 0031208887 scopus 로고    scopus 로고
    • Photophysics of photosynthesis: Structure and spectroscopy of reaction centers of purple bacteria
    • Hoff, A. J., and J. Deisenhofer. 1997. Photophysics of photosynthesis: structure and spectroscopy of reaction centers of purple bacteria. Phys. Rep. Rev. Phys. Lett. 287:247.
    • (1997) Phys. Rep. Rev. Phys. Lett. , vol.287 , pp. 247
    • Hoff, A.J.1    Deisenhofer, J.2
  • 18
    • 0034577649 scopus 로고    scopus 로고
    • Reaction centers of purple bacteria
    • N. S. Scrutton and A. Holzenburg, editors. Kluwer Academic/Plenum Publishers, New York
    • van Brederode, M. E., and M. R. Jones. 2000. Reaction centers of purple bacteria. In Enzyme-Catalyzed Electron and Radical Transfer. N. S. Scrutton and A. Holzenburg, editors. Kluwer Academic/Plenum Publishers, New York. 621-676.
    • (2000) Enzyme-Catalyzed Electron and Radical Transfer , pp. 621-676
    • Van Brederode, M.E.1    Jones, M.R.2
  • 19
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron-proton transfer
    • Stowell, M. H. B., T. M. McPhillips, D. C. Rees, S. M. Soltis, E. Abresch, and G. Feher. 1997. Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Science. 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
  • 21
    • 0034663537 scopus 로고    scopus 로고
    • Re-emerging structures - Continuing crystallography of the bacterial reaction center
    • Fyfe, P. K., and M. R. Jones. 2000. Re-emerging structures - continuing crystallography of the bacterial reaction center. Biochim. Biophys. Acta. 1459:413-421.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 413-421
    • Fyfe, P.K.1    Jones, M.R.2
  • 22
    • 0034671487 scopus 로고    scopus 로고
    • Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-Ångstrom resolution
    • Lancaster, C. R. D., M. V. Bibikova, P. Sabatino, D. Oesterhelt, and H. Michel. 2000. Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-Ångstrom resolution. J. Biol. Chem. 275:39364-39368.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39364-39368
    • Lancaster, C.R.D.1    Bibikova, M.V.2    Sabatino, P.3    Oesterhelt, D.4    Michel, H.5
  • 23
    • 1842502604 scopus 로고    scopus 로고
    • X-ray structure determination of three mutants of the bacterial photosynthetic reaction center from Rb. sphaeroides: Altered proton transfer pathways
    • Xu, Q., H. L. Axelrod, E. C. Abresch, M. L. Paddock, M. Y. Okamura, and G. Feher. 2004. X-ray structure determination of three mutants of the bacterial photosynthetic reaction center from Rb. sphaeroides: altered proton transfer pathways. Structure. 12:703-715.
    • (2004) Structure , vol.12 , pp. 703-715
    • Xu, Q.1    Axelrod, H.L.2    Abresch, E.C.3    Paddock, M.L.4    Okamura, M.Y.5    Feher, G.6
  • 24
    • 0001337010 scopus 로고
    • The pathway, kinetics and thermodynamics of electron transfer in wild-type and mutant bacterial reaction centers of purple nonsulfur bacteria
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer, editors. Kluwer Academic Publishers, The Netherlands
    • Woodbury, N. W., and J. P. Allen. 1995. The pathway, kinetics and thermodynamics of electron transfer in wild-type and mutant bacterial reaction centers of purple nonsulfur bacteria. In Anoxygenic Photosynthetic Bacteria. R. E. Blankenship, M. T. Madigan, and C. E. Bauer, editors. Kluwer Academic Publishers, The Netherlands. 527-557.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 527-557
    • Woodbury, N.W.1    Allen, J.P.2
  • 25
    • 0011920961 scopus 로고
    • Partial purification, subunit structure and thermal stability of the photochemical reaction center of the thermophilic green bacterium Chloroflexus aurantiacus
    • Pierson, B. K., J. P. Thornber, and R. B. Seftor. 1983. Partial purification, subunit structure and thermal stability of the photochemical reaction center of the thermophilic green bacterium Chloroflexus aurantiacus. Biochim. Biophys. Acta. 723:322-326.
    • (1983) Biochim. Biophys. Acta , vol.723 , pp. 322-326
    • Pierson, B.K.1    Thornber, J.P.2    Seftor, R.B.3
  • 26
    • 0025994916 scopus 로고
    • Temperature and solvent effects on reaction centers from Chloroflexus aurantiacus and Chromatium tepidum
    • Nozawa, T., and M. T. Madigan. 1991. Temperature and solvent effects on reaction centers from Chloroflexus aurantiacus and Chromatium tepidum. J. Biochem. (Tokyo). 110:588-594.
    • (1991) J. Biochem. (Tokyo) , vol.110 , pp. 588-594
    • Nozawa, T.1    Madigan, M.T.2
  • 27
    • 0029230320 scopus 로고
    • Effect of temperature on optical properties of reaction centers organized in Langmuir-Blodgett films
    • Antolini, F., M. Trotta, and C. Nicolini. 1995. Effect of temperature on optical properties of reaction centers organized in Langmuir-Blodgett films. Thin Solid Films. 254:252-256.
    • (1995) Thin Solid Films , vol.254 , pp. 252-256
    • Antolini, F.1    Trotta, M.2    Nicolini, C.3
  • 28
    • 0036594522 scopus 로고    scopus 로고
    • Light- And redox-dependent thermal stability of the reaction center of the photosynthetic bacterium Rhodobacter sphaeroides
    • Tokaji, Z., J. Tandori, and P. Maroti. 2002. Light- and redox-dependent thermal stability of the reaction center of the photosynthetic bacterium Rhodobacter sphaeroides. Photochem. Photobiol. 75:605-612.
    • (2002) Photochem. Photobiol. , vol.75 , pp. 605-612
    • Tokaji, Z.1    Tandori, J.2    Maroti, P.3
  • 29
    • 0028331145 scopus 로고
    • Site-specific mutagenesis of the reaction center from Rhodobacter sphaeroides studied by Fourier-transform Raman spectroscopy - Mutations at Tyrosine M210 do not affect the electronic structure of the primary donor
    • Jones, M. R., M. Heerdawson, T. A. Mattioli, C. N. Hunter, and B. Robert. 1994. Site-specific mutagenesis of the reaction center from Rhodobacter sphaeroides studied by Fourier-transform Raman spectroscopy - mutations at Tyrosine M210 do not affect the electronic structure of the primary donor. FEBS Lett. 339:18-24.
    • (1994) FEBS Lett. , vol.339 , pp. 18-24
    • Jones, M.R.1    Heerdawson, M.2    Mattioli, T.A.3    Hunter, C.N.4    Robert, B.5
  • 30
    • 0032492681 scopus 로고    scopus 로고
    • Structural studies of wild-type and mutant reaction centers from an antenna-deficient strain of Rhodobacter sphaeroides: Monitoring the optical properties of the complex from bacterial cell to crystal
    • McAuley-Hecht, K. E., P. K. Fyfe, J. P. Ridge, S. M. Prince, C. N. Hunter, N. W. Isaacs, R. J. Cogdell, and M. R. Jones. 1998. Structural studies of wild-type and mutant reaction centers from an antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical properties of the complex from bacterial cell to crystal. Biochemistry. 37:4740-4750.
    • (1998) Biochemistry , vol.37 , pp. 4740-4750
    • McAuley-Hecht, K.E.1    Fyfe, P.K.2    Ridge, J.P.3    Prince, S.M.4    Hunter, C.N.5    Isaacs, N.W.6    Cogdell, R.J.7    Jones, M.R.8
  • 31
    • 0026433393 scopus 로고
    • Langmuir-Blodgett monolayer films of bacterial photosynthetic membranes and isolated reaction centers - Preparation, spectrophotometric and electrochemical characterization. 1
    • Alegria, G., and P. L. Dutton. 1991. Langmuir-Blodgett monolayer films of bacterial photosynthetic membranes and isolated reaction centers - preparation, spectrophotometric and electrochemical characterization. 1. Biochim. Biophys. Acta. 1057:239-257.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 239-257
    • Alegria, G.1    Dutton, P.L.2
  • 32
    • 0002035566 scopus 로고
    • Reducing bias and inefficiency in the selection algorithm
    • Baker, J. E. 1987. Reducing bias and inefficiency in the selection algorithm. Proc. ICGA. 2:14-21.
    • (1987) Proc. ICGA , vol.2 , pp. 14-21
    • Baker, J.E.1
  • 33
    • 0003140039 scopus 로고
    • Predictive models for the breeder genetic algorithm. I. Continuous parameter optimization
    • Mühlenbein, H., and D. Schlierkamp-Voosen. 1993. Predictive models for the breeder genetic algorithm. I. Continuous parameter optimization. Evol. Comput. 1:25-49.
    • (1993) Evol. Comput. , vol.1 , pp. 25-49
    • Mühlenbein, H.1    Schlierkamp-Voosen, D.2
  • 34
    • 0016285532 scopus 로고
    • The pigment complement of the photosynthetic reaction center isolated from Rhodospirillum rubrum
    • Van der Rest, M., and G. Gringas. 1974. The pigment complement of the photosynthetic reaction center isolated from Rhodospirillum rubrum. J. Biol. Chem. 249:6446-6453.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6446-6453
    • Van Der Rest, M.1    Gringas, G.2
  • 35
    • 0002525792 scopus 로고
    • A general theory of coupled sets of first-order reactions
    • Matsen, F. A., and J. L. Franklin. 1950. A general theory of coupled sets of first-order reactions. J. Am. Chem. Soc. 72:3337-3341.
    • (1950) J. Am. Chem. Soc. , vol.72 , pp. 3337-3341
    • Matsen, F.A.1    Franklin, J.L.2
  • 36
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • Lumry, R., and H. Eyring. 1954. Conformation changes of proteins. J. Phys. Chem. 58:110-120.
    • (1954) J. Phys. Chem. , vol.58 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 37
    • 0015918856 scopus 로고
    • Kinetics of unfolding and refolding of proteins
    • Ikai, A., and C. Tanford. 1973. Kinetics of unfolding and refolding of proteins. J. Mol. Biol. 73:145-163.
    • (1973) J. Mol. Biol. , vol.73 , pp. 145-163
    • Ikai, A.1    Tanford, C.2
  • 38
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumrey-Eyring models in differential scanning calorimetry
    • M. Sanchez-Ruiz, J. 1992. Theoretical analysis of Lumrey-Eyring models in differential scanning calorimetry. Biophys. J. 61:921-935.
    • (1992) Biophys. J. , vol.61 , pp. 921-935
    • Sanchez-Ruiz J, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.