메뉴 건너뛰기




Volumn 351, Issue 3, 2005, Pages 573-597

Binding of the respiratory chain inhibitor antimycin to the mitochondrial bc1 complex: A new crystal structure reveals an altered intramolecular hydrogen-bonding pattern

Author keywords

Antimycin; Cytochrome bc1; Inhibitor binding site; Membrane protein complex; Respiratory chain

Indexed keywords

AMIDE; ANTIMYCIN A1; ASPARTIC ACID; CARBONYL DERIVATIVE; CYTOCHROME B; HYDROGEN; LACTONE; LYSINE; NITROGEN; PHENOL; UBIQUINOL CYTOCHROME C REDUCTASE; WATER;

EID: 22544467474     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.05.053     Document Type: Article
Times cited : (239)

References (77)
  • 1
    • 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
  • 2
    • 0020173148 scopus 로고
    • A Q-cycle mechanism for the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides
    • A.R. Crofts, and S.W. Meinhardt A Q-cycle mechanism for the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides Biochem. Soc. Trans. 10 1982 201 203
    • (1982) Biochem. Soc. Trans. , vol.10 , pp. 201-203
    • Crofts, A.R.1    Meinhardt, S.W.2
  • 3
    • 0016690480 scopus 로고
    • 1 complex in the respiratory chain: Protonmotive ubquinone cycle
    • 1 complex in the respiratory chain: protonmotive ubquinone cycle FEBS Letters 56 1975 1 6
    • (1975) FEBS Letters , vol.56 , pp. 1-6
    • Mitchell, P.1
  • 4
    • 0017117023 scopus 로고
    • Evidence for a protonmotive Q cycle mechanism of electron transfer through the cytochrome b-c1 complex
    • B.L. Trumpower Evidence for a protonmotive Q cycle mechanism of electron transfer through the cytochrome b-c1 complex Biochem. Biophys. Res. Commun. 70 1976 73 80
    • (1976) Biochem. Biophys. Res. Commun. , vol.70 , pp. 73-80
    • Trumpower, B.L.1
  • 5
    • 0015911233 scopus 로고
    • The mechanism of action of the respiratory inhibitor, antimycin
    • E.C. Slater The mechanism of action of the respiratory inhibitor, antimycin Biochim. Biophys. Acta 301 1973 129 154
    • (1973) Biochim. Biophys. Acta , vol.301 , pp. 129-154
    • Slater, E.C.1
  • 6
    • 0015526672 scopus 로고
    • The allosteric binding of antimycin to cytochrome b in the mitochondrial membrane
    • J.A. Berden, and E.C. Slater The allosteric binding of antimycin to cytochrome b in the mitochondrial membrane Biochim. Biophys. Acta 256 1972 199 215
    • (1972) Biochim. Biophys. Acta , vol.256 , pp. 199-215
    • Berden, J.A.1    Slater, E.C.2
  • 7
    • 0037510068 scopus 로고
    • Effects of 2,3-dimercaptopropanol and antimycin on absorption spectra of heart-muscle preparations
    • D.H. Deul, and M.B. Thorn Effects of 2,3-dimercaptopropanol and antimycin on absorption spectra of heart-muscle preparations Biochim. Biophys. Acta 59 1962 426 436
    • (1962) Biochim. Biophys. Acta , vol.59 , pp. 426-436
    • Deul, D.H.1    Thorn, M.B.2
  • 8
    • 3042774340 scopus 로고
    • The kinetics and inhibition of cytochrome components of the succinic oxidase system. III. Cytochrome b
    • B. Chance The kinetics and inhibition of cytochrome components of the succinic oxidase system. III. Cytochrome b J. Biol. Chem. 233 1958 1223 1229
    • (1958) J. Biol. Chem. , vol.233 , pp. 1223-1229
    • Chance, B.1
  • 9
    • 0016833680 scopus 로고
    • Controlled reduction of cytochrome b in succinate-cytochrome c reductase complex by succinate in the presence of ascorbate and antimycin
    • B.L. Trumpower, and A. Katki Controlled reduction of cytochrome b in succinate-cytochrome c reductase complex by succinate in the presence of ascorbate and antimycin Biochem. Biophys. Res. Commun. 65 1975 16 23
    • (1975) Biochem. Biophys. Res. Commun. , vol.65 , pp. 16-23
    • Trumpower, B.L.1    Katki, A.2
  • 10
    • 0015506505 scopus 로고
    • Oxidoreduction of cytochrome b in the presence of antimycin
    • M.K. Wikstrom, and J.A. Berden Oxidoreduction of cytochrome b in the presence of antimycin Biochim. Biophys. Acta 283 1972 403 420
    • (1972) Biochim. Biophys. Acta , vol.283 , pp. 403-420
    • Wikstrom, M.K.1    Berden, J.A.2
  • 11
    • 0017879979 scopus 로고
    • The preparation and characterization of highly purified, enzymically active complex III from baker's yeast
    • J.N. Siedow, S. Power, F.F. de la Rosa, and G. Palmer The preparation and characterization of highly purified, enzymically active complex III from baker's yeast J. Biol. Chem. 253 1978 2392 2399
    • (1978) J. Biol. Chem. , vol.253 , pp. 2392-2399
    • Siedow, J.N.1    Power, S.2    De La Rosa, F.F.3    Palmer, G.4
  • 12
    • 0017882093 scopus 로고
    • Evidence for the existence of a ubiquinone protein and its radical in the cytochromes b and c1 region in the mitochondrial electron transport chain
    • C.A. Yu, S. Nagaoka, L. Yu, and T.E. King Evidence for the existence of a ubiquinone protein and its radical in the cytochromes b and c1 region in the mitochondrial electron transport chain Biochem. Biophys. Res. Commun. 82 1978 1070 1078
    • (1978) Biochem. Biophys. Res. Commun. , vol.82 , pp. 1070-1078
    • Yu, C.A.1    Nagaoka, S.2    Yu, L.3    King, T.E.4
  • 13
    • 0014199203 scopus 로고
    • On the antimycin-sensitive cleavage of complex 3 of the mitochondrial respiratory chain
    • J.S. Rieske, H. Baum, C.D. Stoner, and S.H. Lipton On the antimycin-sensitive cleavage of complex 3 of the mitochondrial respiratory chain J. Biol. Chem. 242 1967 4854 4866
    • (1967) J. Biol. Chem. , vol.242 , pp. 4854-4866
    • Rieske, J.S.1    Baum, H.2    Stoner, C.D.3    Lipton, S.H.4
  • 14
    • 0017594519 scopus 로고
    • Binding of HQNO to beef-heart sub-mitochondrial particles
    • G. Van Ark, and J.A. Berden Binding of HQNO to beef-heart sub-mitochondrial particles Biochim. Biophys. Acta 459 1977 119 127
    • (1977) Biochim. Biophys. Acta , vol.459 , pp. 119-127
    • Van Ark, G.1    Berden, J.A.2
  • 15
    • 0345315746 scopus 로고
    • On the mechanism of electron transfer in complex III of the electron transfer chain
    • H. Baum, J.S. Rieske, H.I. Silman, and S.H. Lipton On the mechanism of electron transfer in complex III of the electron transfer chain Proc. Natl Acad. Sci. USA 57 1967 798 805
    • (1967) Proc. Natl Acad. Sci. USA , vol.57 , pp. 798-805
    • Baum, H.1    Rieske, J.S.2    Silman, H.I.3    Lipton, S.H.4
  • 16
    • 0019175451 scopus 로고
    • Inhibitors of respiration at energy-coupling site 2 of the respiratory chain
    • J.S. Rieske Inhibitors of respiration at energy-coupling site 2 of the respiratory chain Pharmacol. Ther. 11 1980 415 450
    • (1980) Pharmacol. Ther. , vol.11 , pp. 415-450
    • Rieske, J.S.1
  • 17
    • 0034687715 scopus 로고    scopus 로고
    • Proteolytic cleavage of the Fe-S subunit hinge region of Rhodobacter capsulatus bc(1) complex: Effects of inhibitors and mutations
    • M. Valkova-Valchanova, E. Darrouzet, C.R. Moomaw, C.A. Slaughter, and F. Daldal Proteolytic cleavage of the Fe-S subunit hinge region of Rhodobacter capsulatus bc(1) complex: effects of inhibitors and mutations Biochemistry 39 2000 15484 15492
    • (2000) Biochemistry , vol.39 , pp. 15484-15492
    • Valkova-Valchanova, M.1    Darrouzet, E.2    Moomaw, C.R.3    Slaughter, C.A.4    Daldal, F.5
  • 18
    • 2442538306 scopus 로고    scopus 로고
    • Anti-cooperative oxidation of ubiquinol by the yeast cytochrome bc1 complex
    • R. Covian, E.B. Gutierrez-Cirlos, and B.L. Trumpower Anti-cooperative oxidation of ubiquinol by the yeast cytochrome bc1 complex J. Biol. Chem. 279 2004 15040 15049
    • (2004) J. Biol. Chem. , vol.279 , pp. 15040-15049
    • Covian, R.1    Gutierrez-Cirlos, E.B.2    Trumpower, B.L.3
  • 21
    • 0032311167 scopus 로고    scopus 로고
    • o) of the cytochrome bc1 complex
    • o) of the cytochrome bc1 complex Biochim. Biophys. Acta 1365 1998 261 268
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 261-268
    • Brandt, U.1
  • 22
    • 0032733682 scopus 로고    scopus 로고
    • o) of the cytochrome bc1 complex
    • o) of the cytochrome bc1 complex J. Bioenerg. Biomembr. 31 1999 243 250
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 243-250
    • Brandt, U.1
  • 23
    • 0032760483 scopus 로고    scopus 로고
    • Structure of the avian mitochondrial cytochrome bc1 complex
    • E.A. Berry, L.S. Huang, Z. Zhang, and S.H. Kim Structure of the avian mitochondrial cytochrome bc1 complex J. Bioenerg. Biomembr. 31 1999 177 190
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 177-190
    • Berry, E.A.1    Huang, L.S.2    Zhang, Z.3    Kim, S.H.4
  • 24
    • 0043167790 scopus 로고    scopus 로고
    • Structural basis for the quinone reduction in the bc(1) complex: A comparative analysis of crystal structures of mitochondrial cytochrome bc(1) with bound substrate and inhibitors at the Q(i) site
    • X. Gao, X. Wen, L. Esser, B. Quinn, L. Yu, C.A. Yu, and D. Xia Structural basis for the quinone reduction in the bc(1) complex: a comparative analysis of crystal structures of mitochondrial cytochrome bc(1) with bound substrate and inhibitors at the Q(i) site Biochemistry 42 2003 9067 9080
    • (2003) Biochemistry , vol.42 , pp. 9067-9080
    • Gao, X.1    Wen, X.2    Esser, L.3    Quinn, B.4    Yu, L.5    Yu, C.A.6    Xia, D.7
  • 25
    • 0018785572 scopus 로고
    • The multiplicity and stoichiometry of the prosthetic groups in QH2: Cytochrome c oxidoreductase as studied by EPR
    • S. de Vries, S.P. Albracht, and F.J. Leeuwerik The multiplicity and stoichiometry of the prosthetic groups in QH2: cytochrome c oxidoreductase as studied by EPR Biochim. Biophys. Acta 546 1979 316 333
    • (1979) Biochim. Biophys. Acta , vol.546 , pp. 316-333
    • De Vries, S.1    Albracht, S.P.2    Leeuwerik, F.J.3
  • 26
    • 0021759930 scopus 로고
    • Reduction of cytochrome b-561 through the antimycin-sensitive site of the ubiquinol-cytochrome c2 oxidoreductase complex of Rhodopseudomonas sphaeroides
    • E.G. Glaser, S.W. Meinhardt, and A.R. Crofts Reduction of cytochrome b-561 through the antimycin-sensitive site of the ubiquinol-cytochrome c2 oxidoreductase complex of Rhodopseudomonas sphaeroides FEBS Letters 178 1984 336 342
    • (1984) FEBS Letters , vol.178 , pp. 336-342
    • Glaser, E.G.1    Meinhardt, S.W.2    Crofts, A.R.3
  • 27
    • 0007715338 scopus 로고
    • A new effect of antimycin on the b-cytochromes of Rps. Sphaeroides
    • C. Sybesma Martinus Nijhoff/Junk Publishers The Hague
    • S.W. Meinhardt, and A.R. Crofts A new effect of antimycin on the b-cytochromes of Rps. Sphaeroides C. Sybesma Advances in Photosynthesis Research vol. 1 1984 Martinus Nijhoff/Junk Publishers The Hague 649 652
    • (1984) Advances in Photosynthesis Research , vol.1 , pp. 649-652
    • Meinhardt, S.W.1    Crofts, A.R.2
  • 28
    • 0021368185 scopus 로고
    • Thermodynamic properties of the semiquinone and its binding site in the ubiquinol-cytochrome c (c2) oxidoreductase of respiratory and photosynthetic systems
    • D.E. Robertson, R.C. Prince, J.R. Bowyer, K. Matsuura, P.L. Dutton, and T. Ohnishi Thermodynamic properties of the semiquinone and its binding site in the ubiquinol-cytochrome c (c2) oxidoreductase of respiratory and photosynthetic systems J. Biol. Chem. 259 1984 1758 1763
    • (1984) J. Biol. Chem. , vol.259 , pp. 1758-1763
    • Robertson, D.E.1    Prince, R.C.2    Bowyer, J.R.3    Matsuura, K.4    Dutton, P.L.5    Ohnishi, T.6
  • 29
    • 0024432573 scopus 로고
    • Thermodynamic and spectroscopic characteristics of the cytochrome bc1 complex. Role of quinone in the behavior of cytochrome b562
    • J.C. Salerno, Y. Xu, M.P. Osgood, C.H. Kim, and T.E. King Thermodynamic and spectroscopic characteristics of the cytochrome bc1 complex. Role of quinone in the behavior of cytochrome b562 J. Biol. Chem. 264 1989 15398 15403
    • (1989) J. Biol. Chem. , vol.264 , pp. 15398-15403
    • Salerno, J.C.1    Xu, Y.2    Osgood, M.P.3    Kim, C.H.4    King, T.E.5
  • 30
    • 0025316271 scopus 로고
    • Inhibitor effects on redox-linked protonations of the b haems of the mitochondrial bc1 complex
    • P.R. Rich, A.E. Jeal, S.A. Madgwick, and A.J. Moody Inhibitor effects on redox-linked protonations of the b haems of the mitochondrial bc1 complex Biochim. Biophys. Acta 1018 1990 29 40
    • (1990) Biochim. Biophys. Acta , vol.1018 , pp. 29-40
    • Rich, P.R.1    Jeal, A.E.2    Madgwick, S.A.3    Moody, A.J.4
  • 32
    • 0021097527 scopus 로고
    • Effect of b-c1-site inhibitors on the midpoint potentials of mitochondrial cytochromes b
    • W.S. Kunz, and A.A. Konstantinov Effect of b-c1-site inhibitors on the midpoint potentials of mitochondrial cytochromes b FEBS Letters 155 1983 237 240
    • (1983) FEBS Letters , vol.155 , pp. 237-240
    • Kunz, W.S.1    Konstantinov, A.A.2
  • 33
    • 1942437620 scopus 로고    scopus 로고
    • Hydrogen bonds involved in binding the Qi-site semiquinone in the bc1 complex, identified through deuterium exchange using pulsed EPR
    • S.A. Dikanov, R.I. Samoilova, D.R. Kolling, J.T. Holland, and A.R. Crofts Hydrogen bonds involved in binding the Qi-site semiquinone in the bc1 complex, identified through deuterium exchange using pulsed EPR J. Biol. Chem. 279 2004 15814 15823
    • (2004) J. Biol. Chem. , vol.279 , pp. 15814-15823
    • Dikanov, S.A.1    Samoilova, R.I.2    Kolling, D.R.3    Holland, J.T.4    Crofts, A.R.5
  • 34
    • 0034752751 scopus 로고    scopus 로고
    • The biochemical mode of action of the novel selective fungicide cyazofamid: Specific inhibition of mitochondrial complex III in Phythium spinosum
    • S. Mitani, S. Araki, Y. Takii, T. Ohshima, N. Matsuo, and H. Miyoshi The biochemical mode of action of the novel selective fungicide cyazofamid: specific inhibition of mitochondrial complex III in Phythium spinosum Pestic. Biochem. Physiol. 71 2001 107 115(9)
    • (2001) Pestic. Biochem. Physiol. , vol.71 , pp. 107-1159
    • Mitani, S.1    Araki, S.2    Takii, Y.3    Ohshima, T.4    Matsuo, N.5    Miyoshi, H.6
  • 35
    • 4043176359 scopus 로고    scopus 로고
    • Development of a novel fungicide, cyazofamid
    • Mitani, S.; Matsuo, N.; Nakajima, T.
    • Ohshima, T. & Komyoji, T. (2004). Development of a novel fungicide, cyazofamid. Mitani, S.; Matsuo, N.; Nakajima, T. J. Pestic. Sci, 29, 136-138.
    • (2004) J. Pestic. Sci , vol.29 , pp. 136-138
    • Ohshima, T.1    Komyoji, T.2
  • 36
    • 0001003965 scopus 로고
    • The chemistry of antimycin A. Xi. N-substituted 3-formamidosalicylic amides
    • J.P. Dickie, M.E. Loomans, T.M. Farley, and F.M. Strong The chemistry of antimycin A. Xi. N-substituted 3-formamidosalicylic amides J. Med. Chem. 122 1963 424 427
    • (1963) J. Med. Chem. , vol.122 , pp. 424-427
    • Dickie, J.P.1    Loomans, M.E.2    Farley, T.M.3    Strong, F.M.4
  • 37
    • 0025998585 scopus 로고
    • Inhibition of electron transport of rat liver mitochondria by unnatural (-)-antimycin A3
    • H. Miyoshi, H. Kondo, T. Oritani, I. Saitoh, and H. Iwamura Inhibition of electron transport of rat liver mitochondria by unnatural (-)-antimycin A3 FEBS Letters 292 1991 61 63
    • (1991) FEBS Letters , vol.292 , pp. 61-63
    • Miyoshi, H.1    Kondo, H.2    Oritani, T.3    Saitoh, I.4    Iwamura, H.5
  • 38
    • 0028927424 scopus 로고
    • A model of antimycin a binding based on structure-activity studies of synthetic antimycin a analogues
    • H. Miyoshi, N. Tokutake, Y. Imaeda, T. Akagi, and H. Iwamura A model of antimycin A binding based on structure-activity studies of synthetic antimycin A analogues Biochim. Biophys. Acta 1229 1995 149 154
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 149-154
    • Miyoshi, H.1    Tokutake, N.2    Imaeda, Y.3    Akagi, T.4    Iwamura, H.5
  • 39
    • 0027273524 scopus 로고
    • Inhibition of electron transport of rat-liver mitochondria by synthesized antimycin a analogs
    • N. Tokutake, H. Miyoshi, H. Nakazato, and H. Iwamura Inhibition of electron transport of rat-liver mitochondria by synthesized antimycin A analogs Biochim. Biophys. Acta 1142 1993 262 268
    • (1993) Biochim. Biophys. Acta , vol.1142 , pp. 262-268
    • Tokutake, N.1    Miyoshi, H.2    Nakazato, H.3    Iwamura, H.4
  • 41
    • 0015182717 scopus 로고
    • Inhibition of electron transport by substituted salicyl-N-(n-octadecyl) amides
    • N. Neft, and T.M. Farley Inhibition of electron transport by substituted salicyl-N-(n-octadecyl)amides J. Med. Chem. 14 1971 1169 1170
    • (1971) J. Med. Chem. , vol.14 , pp. 1169-1170
    • Neft, N.1    Farley, T.M.2
  • 42
    • 0033606283 scopus 로고    scopus 로고
    • Structure of antimycin A1, a specific electron transfer inhibitor of ubiquinol-cytochrome c oxidoreductase
    • H. Kim, L. Esser, M.B. Hossain, D. Xia, C.-A. Yu, and J. Rizo Structure of antimycin A1, a specific electron transfer inhibitor of ubiquinol-cytochrome c oxidoreductase J. Am. Chem. Soc. 121 1999 4902 4903
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4902-4903
    • Kim, H.1    Esser, L.2    Hossain, M.B.3    Xia, D.4    Yu, C.-A.5    Rizo, J.6
  • 45
    • 0024549277 scopus 로고
    • Analysis of antimycin a by reversed-phase liquid chromatography/nuclear magnetic resonance spectrometry
    • S.T. Ha, C.L. Wilkins, and S.L. Abidi Analysis of antimycin A by reversed-phase liquid chromatography/nuclear magnetic resonance spectrometry Anal. Chem. 61 1989 404 408
    • (1989) Anal. Chem. , vol.61 , pp. 404-408
    • Ha, S.T.1    Wilkins, C.L.2    Abidi, S.L.3
  • 46
    • 0030867866 scopus 로고    scopus 로고
    • Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria [published erratum appears in Science 1997 Dec 19;278(5346):2037]
    • D. Xia, C.A. Yu, H. Kim, J.Z. Xia, A.M. Kachurin, and L. Zhang Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria [published erratum appears in Science 1997 Dec 19;278(5346):2037] Science 277 1997 60 66
    • (1997) Science , vol.277 , pp. 60-66
    • Xia, D.1    Yu, C.A.2    Kim, H.3    Xia, J.Z.4    Kachurin, A.M.5    Zhang, L.6
  • 47
    • 0035066836 scopus 로고    scopus 로고
    • Global indicators of X-ray data quality
    • M.S. Weiss Global indicators of X-ray data quality J. Appl. Crystallog. 34 2001 130 135
    • (2001) J. Appl. Crystallog. , vol.34 , pp. 130-135
    • Weiss, M.S.1
  • 48
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • A.A. Vaguine, J. Richelle, and S.J. Wodak SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model Acta Crystallog. sect. D 55 1999 191 205
    • (1999) Acta Crystallog. Sect. D , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 49
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 51
    • 0032479524 scopus 로고    scopus 로고
    • Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex
    • S. Iwata, J.W. Lee, K. Okada, J.K. Lee, M. Iwata, and B. Rasmussen Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex Science 281 1998 64 71
    • (1998) Science , vol.281 , pp. 64-71
    • Iwata, S.1    Lee, J.W.2    Okada, K.3    Lee, J.K.4    Iwata, M.5    Rasmussen, B.6
  • 52
    • 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
    • C. Hunte, J. Koepke, C. Lange, T. Rossmanith, and H. Michel Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment Struct. Fold. Des. 8 2000 669 684
    • (2000) Struct. Fold. Des. , vol.8 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Rossmanith, T.4    Michel, H.5
  • 53
    • 0014199189 scopus 로고
    • A new protein component of complex 3 of the mitochondrial electron transfer chain
    • H.I. Silman, J.S. Rieske, S.H. Lipton, and H. Baum A new protein component of complex 3 of the mitochondrial electron transfer chain J. Biol. Chem. 242 1967 4867 4875
    • (1967) J. Biol. Chem. , vol.242 , pp. 4867-4875
    • Silman, H.I.1    Rieske, J.S.2    Lipton, S.H.3    Baum, H.4
  • 54
    • 0028786596 scopus 로고
    • Ubiquinol-cytochrome-c reductase from human and bovine mitochondria
    • H. Schagger, U. Brandt, S. Gencic, and G. von Jagow Ubiquinol-cytochrome- c reductase from human and bovine mitochondria Methods Enzymol. 260 1995 82 96
    • (1995) Methods Enzymol. , vol.260 , pp. 82-96
    • Schagger, H.1    Brandt, U.2    Gencic, S.3    Von Jagow, G.4
  • 55
    • 0034647038 scopus 로고    scopus 로고
    • Diastereo- and enantioselective total synthesis of stigmatellin a
    • D. Enders, G. Geibel, and S. Osborne Diastereo- and enantioselective total synthesis of stigmatellin A Chemistry 6 2000 1302 1309
    • (2000) Chemistry , vol.6 , pp. 1302-1309
    • Enders, D.1    Geibel, G.2    Osborne, S.3
  • 57
    • 0242405554 scopus 로고    scopus 로고
    • Observations concerning the quinol oxidation site of the cytochrome bc1 complex
    • E.A. Berry, and L.S. Huang Observations concerning the quinol oxidation site of the cytochrome bc1 complex FEBS Letters 555 2003 13 20
    • (2003) FEBS Letters , vol.555 , pp. 13-20
    • Berry, E.A.1    Huang, L.S.2
  • 58
    • 0021773219 scopus 로고
    • Location of haem-binding sites in the mitochondrial cytochrome b
    • M. Saraste Location of haem-binding sites in the mitochondrial cytochrome b FEBS Letters 166 1984 367 372
    • (1984) FEBS Letters , vol.166 , pp. 367-372
    • Saraste, M.1
  • 59
    • 0001311041 scopus 로고
    • Sequence homology and structural similarity between cytochrome b of mitochondrial complex III and the chloroplast b6-f complex: Position of the cytochrome b hemes in the membrane
    • W.R. Widger, W.A. Cramer, R.G. Herrmann, and A. Trebst Sequence homology and structural similarity between cytochrome b of mitochondrial complex III and the chloroplast b6-f complex: position of the cytochrome b hemes in the membrane Proc. Natl Acad. Sci. USA 81 1984 674 678
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 674-678
    • Widger, W.R.1    Cramer, W.A.2    Herrmann, R.G.3    Trebst, A.4
  • 60
    • 0002320878 scopus 로고
    • Catalytic sites for reduction and oxidation of quinones
    • S. Papa Plenum Press New York
    • A. Crofts, H. Robinson, K. Andrews, S. van Doren, and E. Berry Catalytic sites for reduction and oxidation of quinones S. Papa Cytochrome Systems 1988 Plenum Press New York 617 624
    • (1988) Cytochrome Systems , pp. 617-624
    • Crofts, A.1    Robinson, H.2    Andrews, K.3    Van Doren, S.4    Berry, E.5
  • 61
    • 0032830370 scopus 로고    scopus 로고
    • Structures of quinone binding sites in bc complexes: Functional implications
    • E.A. Berry, Z. Zhang, L.S. Huang, and S.H. Kim Structures of quinone binding sites in bc complexes: functional implications Biochem. Soc. Trans. 27 1999 565 572
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 565-572
    • Berry, E.A.1    Zhang, Z.2    Huang, L.S.3    Kim, S.H.4
  • 62
    • 0028178750 scopus 로고
    • Requirement of histidine 217 for ubiquinone reductase activity (Qi site) in the cytochrome bc1 complex
    • K.A. Gray, P.L. Dutton, and F. Daldal Requirement of histidine 217 for ubiquinone reductase activity (Qi site) in the cytochrome bc1 complex Biochemistry 33 1994 723 733
    • (1994) Biochemistry , vol.33 , pp. 723-733
    • Gray, K.A.1    Dutton, P.L.2    Daldal, F.3
  • 63
    • 0027419268 scopus 로고
    • Comparison between the properties of 3-nitrosalicyl-N-alkylamide and antimycin a acting on QH2:cytochrome c reductase
    • J.X. Xu, Y. Xiao, Y.H. Wang, X. Li, and L.Q. Gu Comparison between the properties of 3-nitrosalicyl-N-alkylamide and antimycin A acting on QH2:cytochrome c reductase Biochim. Biophys. Acta 1142 1993 83 87
    • (1993) Biochim. Biophys. Acta , vol.1142 , pp. 83-87
    • Xu, J.X.1    Xiao, Y.2    Wang, Y.H.3    Li, X.4    Gu, L.Q.5
  • 64
    • 0037022594 scopus 로고    scopus 로고
    • Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c
    • C. Lange, and C. Hunte Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c Proc. Natl Acad. Sci. USA 99 2002 2800 2805
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 2800-2805
    • Lange, C.1    Hunte, C.2
  • 65
    • 0037055971 scopus 로고    scopus 로고
    • Electron transfer between yeast cytochrome bc(1) complex and cytochrome c: A structural analysis
    • C. Hunte, S. Solmaz, and C. Lange Electron transfer between yeast cytochrome bc(1) complex and cytochrome c: a structural analysis Biochim. Biophys. Acta 1555 2002 21 28
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 21-28
    • Hunte, C.1    Solmaz, S.2    Lange, C.3
  • 66
    • 0036786230 scopus 로고    scopus 로고
    • The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: The role of aromatic-aromatic interaction in inhibition
    • X. Gao, X. Wen, C. Yu, L. Esser, S. Tsao, and B. Quinn The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition Biochemistry 41 2002 11692 11702
    • (2002) Biochemistry , vol.41 , pp. 11692-11702
    • Gao, X.1    Wen, X.2    Yu, C.3    Esser, L.4    Tsao, S.5    Quinn, B.6
  • 68
    • 0034049451 scopus 로고    scopus 로고
    • Antimycin a resistance in a mutant Leishmania tarentolae strain is correlated to a point mutation in the mitochondrial apocytochrome b gene
    • A. Schnaufer, S. Sbicego, and B. Blum Antimycin A resistance in a mutant Leishmania tarentolae strain is correlated to a point mutation in the mitochondrial apocytochrome b gene Curr. Genet. 37 2000 234 241
    • (2000) Curr. Genet. , vol.37 , pp. 234-241
    • Schnaufer, A.1    Sbicego, S.2    Blum, B.3
  • 70
    • 0025768975 scopus 로고
    • Ubiquinol-cytochrome c oxidoreductase of higher plants. Isolation and characterization of the bc1 complex from potato tuber mitochondria
    • E.A. Berry, L.S. Huang, and V.J. DeRose Ubiquinol-cytochrome c oxidoreductase of higher plants. Isolation and characterization of the bc1 complex from potato tuber mitochondria J. Biol. Chem. 266 1991 9064 9077
    • (1991) J. Biol. Chem. , vol.266 , pp. 9064-9077
    • Berry, E.A.1    Huang, L.S.2    Derose, V.J.3
  • 71
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W.J. Carter R.M. Sweet Academic Press New York
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode C.W.J. Carter R.M. Sweet Macromolecular Crystallography vol. 276 1997 Academic Press New York 307 326
    • (1997) Macromolecular Crystallography , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 72
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • A.T. Brunger The free R value: a novel statistical quantity for assessing the accuracy of crystal structures Nature 355 1992 472 474
    • (1992) Nature , vol.355 , pp. 472-474
    • Brunger, A.T.1
  • 73
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors on these models
    • T.A. Jones, J.-Y. Zhou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors on these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zhou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 77
    • 4043152888 scopus 로고    scopus 로고
    • X-ray structure of Rhodobacter capsulatus cytochrome bc1: Comparison with its mitochondrial and chloroplast counterparts
    • E.A. Berry, L.-S. Huang, L.K. Saechao, N.G. Pon, M. Valkova-Valchanova, and F. Daldal X-ray structure of Rhodobacter capsulatus cytochrome bc1: comparison with its mitochondrial and chloroplast counterparts Photosynth. Res. 81 2004 251 275
    • (2004) Photosynth. Res. , vol.81 , pp. 251-275
    • Berry, E.A.1    Huang, L.-S.2    Saechao, L.K.3    Pon, N.G.4    Valkova-Valchanova, M.5    Daldal, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.