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Volumn 92, Issue 1, 2007, Pages 17-34

Structural basis for the mechanism of electron bifurcation at the quinol oxidation site of the cytochrome bc1 complex

Author keywords

Conformational changes; Crystal structures; Cytochrome bc1 complex; Electron transfer mechanism; Inhibitor binding

Indexed keywords

BACTERIAL PROTEIN; DUROQUINOL OXIDASE; OXIDOREDUCTASE; UBIQUINOL CYTOCHROME C REDUCTASE; UNCLASSIFIED DRUG;

EID: 34547103230     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-007-9155-3     Document Type: Review
Times cited : (49)

References (60)
  • 3
    • 0026602947 scopus 로고
    • X-ray diffraction by crystals of beef heart ubiquinol: Cytochrome c oxidoreductase
    • Berry EA, Huang L, Earnest T, Jap BK (1992) X-ray diffraction by crystals of beef heart ubiquinol: cytochrome c oxidoreductase. J Mol Biol 224:1161-1166
    • (1992) J Mol Biol , vol.224 , pp. 1161-1166
    • Berry, E.A.1    Huang, L.2    Earnest, T.3    Jap, B.K.4
  • 4
    • 0029108210 scopus 로고
    • A new crytal form of bovine heart ubiquinol:cytochrome c oxidoreductase: Determination of space group and unit-cell parameters
    • Berry EA, Shulmeister VM, Huang LS, Kim SH (1995) A new crytal form of bovine heart ubiquinol:cytochrome c oxidoreductase: determination of space group and unit-cell parameters. Acta Cryst D51:235-239
    • (1995) Acta Cryst , vol.51 , pp. 235-239
    • Berry, E.A.1    Shulmeister, V.M.2    Huang, L.S.3    Kim, S.H.4
  • 6
    • 0019176335 scopus 로고
    • The role of the Rieske iron-sulfur center as the electron donor to ferricytochrome c2 in Rhodopseudomonas sphaeroides
    • Bowyer JR, Dutton PL, Prince RC, Crofts AR (1980) The role of the Rieske iron-sulfur center as the electron donor to ferricytochrome c2 in Rhodopseudomonas sphaeroides. Biochim Biophys Acta 592:445-460
    • (1980) Biochim Biophys Acta , vol.592 , pp. 445-460
    • Bowyer, J.R.1    Dutton, P.L.2    Prince, R.C.3    Crofts, A.R.4
  • 8
    • 0026098570 scopus 로고
    • Analysis of inhibitor binding to the mitochondrial cytochrome c reductase by fluorescence quench titration
    • Brandt U, von Jagow G (1991) Analysis of inhibitor binding to the mitochondrial cytochrome c reductase by fluorescence quench titration. Eur J Biochem 195:163-170
    • (1991) Eur J Biochem , vol.195 , pp. 163-170
    • Brandt, U.1    Von Jagow, G.2
  • 9
    • 0030963762 scopus 로고    scopus 로고
    • Role of deprotonation events in ubihydroquinone:cytochrome c oxidoreductase from bovine heart and yeast mitochondria
    • Brandt U, Okun JG (1997) Role of deprotonation events in ubihydroquinone:cytochrome c oxidoreductase from bovine heart and yeast mitochondria. Biochemistry 36:11234-11240
    • (1997) Biochemistry , vol.36 , pp. 11234-11240
    • Brandt, U.1    Okun, J.G.2
  • 15
    • 0034687792 scopus 로고    scopus 로고
    • Probing the role of the Fe-S subunit hinge region during Q(o) site catalysis in Rhodobacter capsulatus bc(1) complex
    • Darrouzet E, Valkova-Valchanova M, Daldal F (2000a) Probing the role of the Fe-S subunit hinge region during Q(o) site catalysis in Rhodobacter capsulatus bc(1) complex. Biochemistry 39:15475-15483
    • (2000) Biochemistry , vol.39 , pp. 15475-15483
    • Darrouzet, E.1    Valkova-Valchanova, M.2    Daldal, F.3
  • 17
    • 0019877746 scopus 로고
    • A new species of bound ubisemiquinone anion in QH2: Cytochrome c oxidoreductase
    • De Vries S, Albracht SPJ, Berden JA, Slater EC (1981) A new species of bound ubisemiquinone anion in QH2: cytochrome c oxidoreductase. J Biol Chem 256:11996-11998
    • (1981) J Biol Chem , vol.256 , pp. 11996-11998
    • De Vries, S.1    Albracht, S.P.J.2    Berden, J.A.3    Slater, E.C.4
  • 18
    • 0026611757 scopus 로고
    • 1 complex [2Fe-2S] cluster and its interaction with ubiquinone and ubihydroquinone at the Qo site: A double-occupancy Qo site model
    • 1 complex [2Fe-2S] cluster and its interaction with ubiquinone and ubihydroquinone at the Qo site: a double-occupancy Qo site model. Biochemistry 31:3144-3158
    • (1992) Biochemistry , vol.31 , pp. 3144-3158
    • Ding, H.1    Robertson, D.E.2    Daldal, F.3    Dutton, P.L.4
  • 24
    • 0028182530 scopus 로고
    • 1 complex: Comparative studies of yeast mutants and natural inhibitor resistant fungi
    • 1 complex: comparative studies of yeast mutants and natural inhibitor resistant fungi. Biochem Soc Trans 22:203-209
    • (1993) Biochem Soc Trans , vol.22 , pp. 203-209
    • Geier, B.M.1    Haase, U.2    Von Jagow, G.3
  • 25
    • 21644456550 scopus 로고    scopus 로고
    • The iron-sulfur cluster of the Rieske iron-sulfur protein functions as a proton-exiting gate in teh cytochrome bc(1) complex
    • Gurung B, Yu L, Xia D, Yu CA (2005) The iron-sulfur cluster of the Rieske iron-sulfur protein functions as a proton-exiting gate in teh cytochrome bc(1) complex. J Biol Chem 280:24895-24902
    • (2005) J Biol Chem , vol.280 , pp. 24895-24902
    • Gurung, B.1    Yu, L.2    Xia, D.3    Yu, C.A.4
  • 26
    • 22544467474 scopus 로고    scopus 로고
    • 1 complex: A new crystal structure reveals an altered intramolecular hydrogen-bonding pattern
    • 1 complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern. J Mol Biol 351:573-597
    • (2005) J Mol Biol , vol.351 , pp. 573-597
    • Huang, L.1    Cobessi, D.2    Tung, E.Y.3    Berry, E.A.4
  • 27
    • 0034660152 scopus 로고    scopus 로고
    • Structure at 2.3 a resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment
    • Hunte C, Koepke J, Lange C, Rossmanith T, Michel H (2000) Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Structure 15:669-684
    • (2000) Structure , vol.15 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Rossmanith, T.4    Michel, H.5
  • 30
    • 0021830124 scopus 로고
    • The chromone inhibitor stigmatellin - Binding to the ubiquinol oxidation center at the C-side of the mitochondrial membrane
    • von Jagow G, Ohnishi T (1985) The chromone inhibitor stigmatellin - binding to the ubiquinol oxidation center at the C-side of the mitochondrial membrane. FEBS Lett 185:311-315
    • (1985) FEBS Lett , vol.185 , pp. 311-315
    • Von Jagow, G.1    Ohnishi, T.2
  • 33
    • 0242494128 scopus 로고    scopus 로고
    • Structure of the cytochrome b6f complex of oxygenic photosynthesis: Tuning the cavity
    • Kurisu G, Zhang H, Smith JL, Cramer WA (2003) Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science 302:1009-1014
    • (2003) Science , vol.302 , pp. 1009-1014
    • Kurisu, G.1    Zhang, H.2    Smith, J.L.3    Cramer, W.A.4
  • 35
    • 0029126881 scopus 로고
    • 1 complex:improved crystallization and flash-colling of a large membrane protein
    • 1 complex:improved crystallization and flash-colling of a large membrane protein. J Mol Biol 252:15-19
    • (1995) J Mol Biol , vol.252 , pp. 15-19
    • Lee, J.W.1    Chan, M.2    Law, T.V.3    Kwon, H.J.4    Jap, B.K.5
  • 36
    • 0027264504 scopus 로고
    • Cytochrome b-deficient mutants of the ubiquinol-cytochrome c oxidoreductase in Saccharomyces cerevisiae. Consequence for the functional and structural characteristics of the complex
    • Lemesle-Meunier D, Brivet-Chevillotte P, di Rago JP, Slonimski PP, Bruel C, Tron T, Forget N (1993) Cytochrome b-deficient mutants of the ubiquinol-cytochrome c oxidoreductase in Saccharomyces cerevisiae. Consequence for the functional and structural characteristics of the complex. J Biol Chem 268:15626-15632
    • (1993) J Biol Chem , vol.268 , pp. 15626-15632
    • Lemesle-Meunier, D.1    Brivet-Chevillotte, P.2    Di Rago, J.P.3    Slonimski, P.P.4    Bruel, C.5    Tron, T.6    Forget, N.7
  • 37
    • 0019888140 scopus 로고
    • Three-dimensional structure of ubiquinol:cytochrome c reductase from neurospora mitochondria determined by electron microscopy of membrane crystals
    • Leonard K, Wingfield P, Arad T, Weiss H (1981) Three-dimensional structure of ubiquinol:cytochrome c reductase from neurospora mitochondria determined by electron microscopy of membrane crystals. J Mol Biol 149:259-274
    • (1981) J Mol Biol , vol.149 , pp. 259-274
    • Leonard, K.1    Wingfield, P.2    Arad, T.3    Weiss, H.4
  • 38
    • 0030861648 scopus 로고    scopus 로고
    • 1 complex - The 'proton-gated affinity change' machanism
    • 1 complex - the 'proton-gated affinity change' machanism. FEBS Lett 412:257-264
    • (1997) FEBS Lett , vol.412 , pp. 257-264
    • Link, T.A.1
  • 39
    • 0027245581 scopus 로고
    • What information do inhibitors provide about the structure of the hydroquinone oxidation site of ubihydroquinone: Cytochrome c oxidoreductase?
    • Link TA, Haase U, Brandt U, von Jagow G (1993) What information do inhibitors provide about the structure of the hydroquinone oxidation site of ubihydroquinone: cytochrome c oxidoreductase? J Bioenerg Biomembr 25:221-232
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 221-232
    • Link, T.A.1    Haase, U.2    Brandt, U.3    Von Jagow, G.4
  • 40
    • 0028792217 scopus 로고
    • 1 complex in quinone binding and interaction with subunit IV
    • 1 complex in quinone binding and interaction with subunit IV. J Biol Chem 270:28668-28675
    • (1995) J Biol Chem , vol.270 , pp. 28668-28675
    • Mather, M.W.1    Yu, L.2    Yu, C.A.3
  • 41
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • Mitchell P (1976) Possible molecular mechanisms of the protonmotive function of cytochrome systems. J Theor Biol 62:327-367
    • (1976) J Theor Biol , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 43
    • 0033952147 scopus 로고    scopus 로고
    • Mutations in the tether region of the iron-sulfur protein affect the activity and assembly of the cytochrome bc(1) complex of yeast mitochondria
    • Obungu VH, Wang Y, Amyot SM, Gocke CB, Beattie DS (2000) Mutations in the tether region of the iron-sulfur protein affect the activity and assembly of the cytochrome bc(1) complex of yeast mitochondria. Biochim Biophys Acta 1457:36-44
    • (2000) Biochim Biophys Acta , vol.1457 , pp. 36-44
    • Obungu, V.H.1    Wang, Y.2    Amyot, S.M.3    Gocke, C.B.4    Beattie, D.S.5
  • 46
    • 0344497439 scopus 로고    scopus 로고
    • An atypical haem in the cytochrome b(6)f complex
    • Stroebel D, Choquet Y, Popot JL, Picot D (2003) An atypical haem in the cytochrome b(6)f complex. Nature 426:413-418
    • (2003) Nature , vol.426 , pp. 413-418
    • Stroebel, D.1    Choquet, Y.2    Popot, J.L.3    Picot, D.4
  • 53
    • 0034624079 scopus 로고    scopus 로고
    • 1 complex by the formation of the intersubunit disulfide bond between cytochrome b and the iron-sulfur protein
    • 1 complex by the formation of the intersubunit disulfide bond between cytochrome b and the iron-sulfur protein. J Biol Chem 275:38597-38604
    • (2000) J Biol Chem , vol.275 , pp. 38597-38604
    • Xiao, K.1    Yu, L.2    Yu, C.A.3
  • 54
    • 0038757546 scopus 로고    scopus 로고
    • Functional insensitivity of the cytochrome b6f complex to structure changes in the hinge region of the Rieske iron-sulfur protein
    • Yan J, Cramer WA (2003) Functional insensitivity of the cytochrome b6f complex to structure changes in the hinge region of the Rieske iron-sulfur protein. J Biol Chem 278:20925-20933
    • (2003) J Biol Chem , vol.278 , pp. 20925-20933
    • Yan, J.1    Cramer, W.A.2
  • 55
    • 0027310147 scopus 로고
    • Mitochondrial ubiquinol-cytochrome c reductase complex: Crystallization and protein: Ubiquinone interaction
    • Yu CA, Yu L (1993) Mitochondrial ubiquinol-cytochrome c reductase complex: crystallization and protein: ubiquinone interaction. J Bioenerg Biomembr 25:259-273
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 259-273
    • Yu, C.A.1    Yu, L.2
  • 58
    • 0025767785 scopus 로고
    • Crystallization of mitochondrial ubiquinol-cytochrome c reductase
    • Yue WH, Zou YP, Yu L, Yu CA (1991) Crystallization of mitochondrial ubiquinol-cytochrome c reductase. Biochemistry 30:2303-2306
    • (1991) Biochemistry , vol.30 , pp. 2303-2306
    • Yue, W.H.1    Zou, Y.P.2    Yu, L.3    Yu, C.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.