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Volumn 50, Issue 48, 2011, Pages 10462-10472

Photoinitiated electron transfer within the Paracoccus denitrificans cytochrome bc 1 complex: Mobility of the iron-sulfur protein is modulated by the occupant of the Q o site

Author keywords

[No Author keywords available]

Indexed keywords

AZOXYSTROBIN; BIPHASIC; DOMAIN ROTATIONS; ELECTRON TRANSFER; IRON-SULFUR PROTEINS; PARACOCCUS DENITRIFICANS; RATE CONSTANT K; REDOX CENTERS; REDOX POTENTIALS; RELATIVE AMPLITUDE;

EID: 82455172077     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200453r     Document Type: Article
Times cited : (9)

References (68)
  • 1
    • 0028290824 scopus 로고
    • Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation
    • Trumpower, B. L. and Gennis, R. B. (1994) Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: the enzymology of coupling electron transfer reactions to transmembrane proton translocation Annu. Rev. Biochem. 63, 675-716 (Pubitemid 24218646)
    • (1994) Annual Review of Biochemistry , vol.63 , pp. 675-716
    • Trumpower, B.L.1    Gennis, R.B.2
  • 3
    • 0023645713 scopus 로고
    • 1 complex. Nucleotide sequence and homologies between bacterial and mitochondrial subunits
    • 1 complex. Nucleotide sequence and homologies between bacterial and mitochondrial subunits J. Biol. Chem. 262, 13805-13811
    • (1987) J. Biol. Chem. , vol.262 , pp. 13805-13811
    • Kurowski, B.1    Ludwig, B.2
  • 4
    • 0023655323 scopus 로고
    • 1 and c. Equilibrium constants and kinetic probes
    • 1 and c. Equilibrium constants and kinetic probes J. Biol. Chem. 262, 8103-8108
    • (1987) J. Biol. Chem. , vol.262 , pp. 8103-8108
    • Kim, C.H.1    Balny, C.2    King, T.E.3
  • 6
    • 34447643582 scopus 로고    scopus 로고
    • A Novel Approach to Analyze Membrane Proteins by Laser Mass Spectrometry: From Protein Subunits to the Integral Complex
    • DOI 10.1016/j.jasms.2007.04.013, PII S1044030507003741
    • Morgner, N., Kleinschroth, T., Barth, H. D., Ludwig, B., and Brutschy, B. (2007) A novel approach to analyze membrane proteins by laser mass spectrometry: from protein subunits to the integral complex J. Am. Soc. Mass Spectrom. 18, 1429-1438 (Pubitemid 47088995)
    • (2007) Journal of the American Society for Mass Spectrometry , vol.18 , Issue.8 , pp. 1429-1438
    • Morgner, N.1    Kleinschroth, T.2    Barth, H.-D.3    Ludwig, B.4    Brutschy, B.5
  • 7
    • 0016754421 scopus 로고
    • The protonmotive Q cycle: A general formulation
    • Mitchell, P. (1975) The protonmotive Q cycle: a general formulation FEBS Lett. 59, 137-139
    • (1975) FEBS Lett. , vol.59 , pp. 137-139
    • Mitchell, P.1
  • 8
    • 1942447877 scopus 로고    scopus 로고
    • 1 complex: Function in the context of structure
    • DOI 10.1146/annurev.physiol.66.032102.150251
    • 1 complex: function in the context of structure Annu. Rev. Physiol. 66, 689-733 (Pubitemid 40614460)
    • (2004) Annual Review of Physiology , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 20
    • 0034624079 scopus 로고    scopus 로고
    • 1 complex by the formation of an intersubunit disulfide bond between cytochrome b and the iron-sulfur protein
    • DOI 10.1074/jbc.M007444200
    • 1 complex by the formation of an intersubunit disulfide bond between cytochrome b and the iron-sulfur protein J. Biol. Chem. 275, 38597-38604 (Pubitemid 32009188)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.49 , pp. 38597-38604
    • Xia, K.1    Yu, L.2    Yu, C.-A.3
  • 30
    • 79960557326 scopus 로고    scopus 로고
    • Conformationally linked interaction in the cytochrome bc(1) complex between inhibitors of the Q(o) site and the Rieske iron-sulfur protein
    • Berry, E. A. and Huang, L. S. (2011) Conformationally linked interaction in the cytochrome bc(1) complex between inhibitors of the Q(o) site and the Rieske iron-sulfur protein Biochim. Biophys. Acta 1807, 1349-1363
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1349-1363
    • Berry, E.A.1    Huang, L.S.2
  • 31
    • 1442325507 scopus 로고    scopus 로고
    • o Site Occupants and the Head Domain Position of the Fe-S Protein Subunit
    • DOI 10.1021/bi035938u
    • Cooley, J. W., Roberts, A. G., Bowman, M. K., Kramer, D. M., and Daldal, F. (2004) The raised midpoint potential of the [2Fe2S] cluster of cytochrome bc1 is mediated by both the Qo site occupants and the head domain position of the Fe-S protein subunit Biochemistry 43, 2217-2227 (Pubitemid 38279967)
    • (2004) Biochemistry , vol.43 , Issue.8 , pp. 2217-2227
    • Cooley, J.W.1    Roberts, A.G.2    Bowman, M.K.3    Kramer, D.M.4    Daldal, F.5
  • 32
    • 67649229861 scopus 로고    scopus 로고
    • Magnetic interactions sense changes in distance between heme b(L) and the iron-sulfur cluster in cytochrome bc(1)
    • Sarewicz, M., Dutka, M., Froncisz, W., and Osyczka, A. (2009) Magnetic interactions sense changes in distance between heme b(L) and the iron-sulfur cluster in cytochrome bc(1) Biochemistry 48, 5708-5720
    • (2009) Biochemistry , vol.48 , pp. 5708-5720
    • Sarewicz, M.1    Dutka, M.2    Froncisz, W.3    Osyczka, A.4
  • 38
    • 0014699523 scopus 로고
    • Non-symmetrical dielectric relaxation behaviour arising from a simple empirical decay function
    • Williams, G. and Watts, D. C. (1970) Non-symmetrical dielectric relaxation behaviour arising from a simple empirical decay function Trans. Faraday Soc. 66, 80-85
    • (1970) Trans. Faraday Soc. , vol.66 , pp. 80-85
    • Williams, G.1    Watts, D.C.2
  • 40
    • 1342325555 scopus 로고    scopus 로고
    • Reversible redox energy coupling in electron transfer chains
    • DOI 10.1038/nature02242
    • Osyczka, A., Moser, C. C., Daldal, F., and Dutton, P. L. (2004) Reversible redox energy coupling in electron transfer chains Nature 427, 607-612 (Pubitemid 38248474)
    • (2004) Nature , vol.427 , Issue.6975 , pp. 607-612
    • Osyczka, A.1    Moser, C.C.2    Daldal, F.3    Dutton, P.L.4
  • 48
    • 0033539678 scopus 로고    scopus 로고
    • Effect of inhibitors on the ubiquinone binding capacity of the primary energy conversion site in the Rhodobacter capsulatus cytochrome bc(1) complex
    • Sharp, R. E., Gibney, B. R., Palmitessa, A., White, J. L., Dixon, J. A., Moser, C. C., Daldal, F., and Dutton, P. L. (1999) Effect of inhibitors on the ubiquinone binding capacity of the primary energy conversion site in the Rhodobacter capsulatus cytochrome bc(1) complex Biochemistry 38, 14973-14980
    • (1999) Biochemistry , vol.38 , pp. 14973-14980
    • Sharp, R.E.1    Gibney, B.R.2    Palmitessa, A.3    White, J.L.4    Dixon, J.A.5    Moser, C.C.6    Daldal, F.7    Dutton, P.L.8
  • 50
    • 0033619733 scopus 로고    scopus 로고
    • 1 complex from mitochondria and photosynthetic bacteria
    • 1 complex from mitochondria and photosynthetic bacteria Biochemistry 38, 15827-15839 (Pubitemid 129520474)
    • (1999) Biochemistry , vol.38 , Issue.48 , pp. 15827-15839
    • Crofts, A.R.1    Hong, S.2    Zhang, Z.3    Berry, E.A.4
  • 51
    • 77950567917 scopus 로고    scopus 로고
    • 1 complex: Effects on the biophysical properties of the Rieske iron-sulfur protein and on the kinetics of the complex
    • 1 complex: Effects on the biophysical properties of the Rieske iron-sulfur protein and on the kinetics of the complex J. Biol. Chem. 285, 9233-9248
    • (2010) J. Biol. Chem. , vol.285 , pp. 9233-9248
    • Lhee, S.1    Kolling, D.2    Nair, S.3    Dikanov, S.4    Crofts, A.5
  • 52
    • 0037452557 scopus 로고    scopus 로고
    • 1 complex
    • DOI 10.1021/bi026656h
    • 1 complex Biochemistry 42, 1499-1507 (Pubitemid 36205956)
    • (2003) Biochemistry , vol.42 , Issue.6 , pp. 1499-1507
    • Darrouzet, E.1    Daldal, F.2
  • 53
    • 3542991515 scopus 로고    scopus 로고
    • The quinone chemistry of bc complexes
    • DOI 10.1016/j.bbabio.2004.04.021, PII S000527280400146X
    • Rich, P. R. (2004) The quinone chemistry of bc complexes Biochim. Biophys. Acta 1658, 165-171 (Pubitemid 39013247)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1658 , Issue.1-2 , pp. 165-171
    • Rich, P.R.1
  • 56
    • 23244438766 scopus 로고    scopus 로고
    • 1 complex: Reaction mechanism and prevention of short-circuiting
    • DOI 10.1016/j.bbabio.2005.03.009, PII S0005272805000927
    • 1 complex: reaction mechanism and prevention of short-circuiting Biochim. Biophys. Acta 1709, 5-34 (Pubitemid 41096088)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1709 , Issue.1 , pp. 5-34
    • Mulkidjanian, A.Y.1
  • 62
    • 73649089642 scopus 로고    scopus 로고
    • 1 Complex: Enzyme with one inactive monomer is fully active but unable to activate the second ubiquinol oxidation site in response to ligand binding at the ubiquinone reduction site
    • 1 Complex: Enzyme with one inactive monomer is fully active but unable to activate the second ubiquinol oxidation site in response to ligand binding at the ubiquinone reduction site J. Biol. Chem. 285, 502-510
    • (2010) J. Biol. Chem. , vol.285 , pp. 502-510
    • Castellani, M.1    Covian, R.2    Kleinschroth, T.3    Anderka, O.4    Ludwig, B.5    Trumpower, B.6
  • 64
    • 33846029501 scopus 로고    scopus 로고
    • 1 complexes of phototrophic bacteria: Introducing the activated Q-cycle
    • DOI 10.1039/b517522d
    • 1 complexes of phototrophic bacteria: introducing the activated Q-cycle Photochem. Photobiol. Sci. 6, 19-34 (Pubitemid 46046002)
    • (2007) Photochemical and Photobiological Sciences , vol.6 , Issue.1 , pp. 19-34
    • Mulkidjanian, A.Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.