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Volumn 586, Issue 5, 2012, Pages 617-621

Recent advances in cytochrome bc 1: Inter monomer electronic communication?

Author keywords

Cytochrome bc 1; Heterodimer; Inter monomer electron transfer; Q cycle mechanism; Rhodobacter capsulatus

Indexed keywords

CYTOCHROME C OXIDASE; MONOMER;

EID: 84857919298     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.08.032     Document Type: Review
Times cited : (15)

References (38)
  • 3
    • 30144441164 scopus 로고    scopus 로고
    • Understanding the cytochrome bc complexes by what they don't do. The Q-cycle at 30
    • DOI 10.1016/j.tplants.2005.11.007, PII S1360138505002955
    • J.L. Cape, M.K. Bowman, and D.M. Kramer Understanding the cytochrome bc complexes by what they don't do. The Q-cycle at 30 Trends Plant Sci. 11 2006 46 55 (Pubitemid 43053978)
    • (2006) Trends in Plant Science , vol.11 , Issue.1 , pp. 46-55
    • Cape, J.L.1    Bowman, M.K.2    Kramer, D.M.3
  • 4
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • P. Mitchell Possible molecular mechanisms of the protonmotive function of cytochrome systems J. Theor. Biol. 62 1976 327 367
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 8
    • 0034660152 scopus 로고    scopus 로고
    • 1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment
    • DOI 10.1016/S0969-2126(00)00152-0
    • 1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment Structure 8 2000 669 684 (Pubitemid 30409318)
    • (2000) Structure , vol.8 , Issue.6 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Rossmanith, T.4    Michel, H.5
  • 12
    • 0001104663 scopus 로고
    • The role of the quinone pool in the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides: A modified Q-cycle mechanism
    • A.R. Crofts, S.W. Meinhardt, K.R. Jones, and M. Snozzi The role of the quinone pool in the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides: a modified Q-cycle mechanism Biochim. Biophys. Acta 723 1983 202 218
    • (1983) Biochim. Biophys. Acta , vol.723 , pp. 202-218
    • Crofts, A.R.1    Meinhardt, S.W.2    Jones, K.R.3    Snozzi, M.4
  • 16
    • 1342325555 scopus 로고    scopus 로고
    • Reversible redox energy coupling in electron transfer chains
    • DOI 10.1038/nature02242
    • A. Osyczka, C.C. Moser, F. Daldal, and P.L. Dutton Reversible redox energy coupling in electron transfer chains Nature 427 2004 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
  • 17
    • 79956128428 scopus 로고    scopus 로고
    • The Q cycle of cytochrome bc complexes: A structure perspective
    • W.A. Cramer, S.S. Hasan, and E. Yamashita The Q cycle of cytochrome bc complexes: a structure perspective Biochim. Biophys. Acta 1807 2011 788 802
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 788-802
    • Cramer, W.A.1    Hasan, S.S.2    Yamashita, E.3
  • 18
    • 0032540757 scopus 로고    scopus 로고
    • 1 complex of Rhodobacter capsulatus: Ubiquinol oxidation in a dimeric Q-cycle?
    • DOI 10.1016/S0014-5793(98)00768-6, PII S0014579398007686
    • 1 complex of Rhodobacter capsulatus: ubiquinol oxidation in a dimeric Q-cycle? FEBS Lett. 431 1998 291 296 (Pubitemid 28334236)
    • (1998) FEBS Letters , vol.431 , Issue.2 , pp. 291-296
    • Gopta, O.A.1    Feniouk, B.A.2    Junge, W.3    Mulkidjanian, A.Y.4
  • 23
    • 20744443796 scopus 로고    scopus 로고
    • 1 complex dimer is reduced through center N
    • DOI 10.1074/jbc.M413592200
    • 1 complex dimer is reduced through center N J. Biol. Chem. 280 2005 22732 22740 (Pubitemid 40853178)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.24 , pp. 22732-22740
    • Covian, R.1    Trumpower, B.L.2
  • 24
    • 34047201634 scopus 로고    scopus 로고
    • 1 complex dimer is controlled by the energized state and by impaired electron transfer between low and high potential hemes
    • DOI 10.1016/j.febslet.2007.03.037, PII S0014579307003031
    • 1 complex dimer is controlled by the energized state and by impaired electron transfer between low and high potential hemes FEBS Lett. 581 2007 1535 1541 (Pubitemid 46541686)
    • (2007) FEBS Letters , vol.581 , Issue.8 , pp. 1535-1541
    • Shinkarev, V.P.1    Wraight, C.A.2
  • 25
    • 0037059734 scopus 로고    scopus 로고
    • 1 complex: Evidence for an alternating, half-of-the-sites mechanism of ubiquinol oxidation
    • DOI 10.1074/jbc.M109097200
    • 1 complex. Evidence for an alternating, half-of-the-sites mechanism of ubiquinol oxidation J. Biol. Chem. 277 2002 1195 1202 (Pubitemid 34968868)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.2 , pp. 1195-1202
    • Gutierrez-Cirlos, E.B.1    Trumpower, B.L.2
  • 27
    • 34547962129 scopus 로고    scopus 로고
    • 1 complex: Evidence for anti-cooperative ubiquinol oxidation and communication between center P ubiquinol oxidation sites
    • DOI 10.1074/jbc.M702132200
    • 1 complex: evidence for anti-cooperative ubiquinol oxidation and communication between center P ubiquinol oxidation sites J. Biol. Chem. 282 2007 22289 22297 (Pubitemid 47267334)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.31 , pp. 22289-22297
    • Covian, R.1    Kleinschroth, T.2    Ludwig, B.3    Trumpower, B.L.4
  • 28
    • 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 2010 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.L.6
  • 34
    • 0242692609 scopus 로고    scopus 로고
    • The Bacterial RecA Protein as a Motor Protein
    • DOI 10.1146/annurev.micro.57.030502.090953
    • M.M. Cox The bacterial RecA protein as a motor protein Annu. Rev. Microbiol. 57 2003 551 577 (Pubitemid 37392955)
    • (2003) Annual Review of Microbiology , vol.57 , pp. 551-577
    • Cox, M.M.1
  • 37
    • 46449118774 scopus 로고    scopus 로고
    • 1 complex account for the function of a dimeric complex?
    • 1 complex account for the function of a dimeric complex? Biochim. Biophys. Acta 1777 2008 1001 1019
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1001-1019
    • Crofts, A.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.