메뉴 건너뛰기




Volumn 121, Issue 7, 2005, Pages 1043-1057

Crystal structure of mitochondrial respiratory membrane protein Complex II

Author keywords

[No Author keywords available]

Indexed keywords

3 NITROPROPIONIC ACID; FLAVOPROTEIN; IRON SULFUR PROTEIN; MEMBRANE PROTEIN; MEMBRANE PROTEIN CYBL; MEMBRANE PROTEIN CYBS; MITOCHONDRIAL PROTEIN; MITOCHONDRIAL PROTEIN COMPLEX II; PROTEIN INHIBITOR; SUCCINIC ACID; THENOYLTRIFLUOROACETONE; UBIQUINONE; UNCLASSIFIED DRUG;

EID: 21244503033     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2005.05.025     Document Type: Article
Times cited : (676)

References (57)
  • 1
    • 0028114231 scopus 로고
    • Structure at 2.8 a resolution of F1-ATPase from bovine heart mitochondria
    • J.P. Abrahams, A.G. Leslie, R. Lutter, and J.E. Walker Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria Nature 370 1994 621 628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 2
    • 0036805853 scopus 로고    scopus 로고
    • Cytopathies involving mitochondrial complex II
    • B.A. Ackrell Cytopathies involving mitochondrial complex II Mol. Aspects Med. 23 2002 369 384
    • (2002) Mol. Aspects Med. , vol.23 , pp. 369-384
    • Ackrell, B.A.1
  • 8
    • 0033840193 scopus 로고    scopus 로고
    • Late-onset optic atrophy, ataxia, and myopathy associated with a mutation of a complex II gene
    • M.A. Birch-Machin, R.W. Taylor, B. Cochran, B.A. Ackrell, and D.M. Turnbull Late-onset optic atrophy, ataxia, and myopathy associated with a mutation of a complex II gene Ann. Neurol. 48 2000 330 335
    • (2000) Ann. Neurol. , vol.48 , pp. 330-335
    • Birch-Machin, M.A.1    Taylor, R.W.2    Cochran, B.3    Ackrell, B.A.4    Turnbull, D.M.5
  • 11
    • 0242391866 scopus 로고    scopus 로고
    • SDHD mutations in head and neck paragangliomas result in destabilization of complex II in the mitochondrial respiratory chain with loss of enzymatic activity and abnormal mitochondrial morphology
    • P.B. Douwes Dekker, P.C. Hogendoorn, N. Kuipers-Dijkshoorn, F.A. Prins, S.G. van Duinen, P.E. Taschner, A.G. van der Mey, and C.J. Cornelisse SDHD mutations in head and neck paragangliomas result in destabilization of complex II in the mitochondrial respiratory chain with loss of enzymatic activity and abnormal mitochondrial morphology J. Pathol. 201 2003 480 486
    • (2003) J. Pathol. , vol.201 , pp. 480-486
    • Douwes Dekker, P.B.1    Hogendoorn, P.C.2    Kuipers-Dijkshoorn, N.3    Prins, F.A.4    Van Duinen, S.G.5    Taschner, P.E.6    Van Der Mey, A.G.7    Cornelisse, C.J.8
  • 12
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. (1997). An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15, 132-134, 112-113.
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 13
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • P. Gouet, E. Courcelle, D.I. Stuart, and F. Metoz ESPript: analysis of multiple sequence alignments in PostScript Bioinformatics 15 1999 305 308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 14
    • 0346850862 scopus 로고    scopus 로고
    • The ubiquinone-binding site of the Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase is a source of superoxide
    • J. Guo, and B.D. Lemire The ubiquinone-binding site of the Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase is a source of superoxide J. Biol. Chem. 278 2003 47629 47635
    • (2003) J. Biol. Chem. , vol.278 , pp. 47629-47635
    • Guo, J.1    Lemire, B.D.2
  • 15
    • 0343052744 scopus 로고    scopus 로고
    • Succinate: Quinone oxidoreductases. Variations on a conserved theme
    • C. Hagerhall Succinate: quinone oxidoreductases. Variations on a conserved theme Biochim. Biophys. Acta 1320 1997 107 141
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 107-141
    • Hagerhall, C.1
  • 16
    • 0017193364 scopus 로고
    • Studies on electron paramagnetic resonance spectra manifested by a respiratory chain hydrogen carrier
    • W.J. Ingledew, J.C. Salerno, and T. Ohnishi Studies on electron paramagnetic resonance spectra manifested by a respiratory chain hydrogen carrier Arch. Biochem. Biophys. 177 1976 176 184
    • (1976) Arch. Biochem. Biophys. , vol.177 , pp. 176-184
    • Ingledew, W.J.1    Salerno, J.C.2    Ohnishi, T.3
  • 18
    • 0033580880 scopus 로고    scopus 로고
    • Structure of the Escherichia coli fumarate reductase respiratory complex
    • T.M. Iverson, C. Luna-Chavez, G. Cecchini, and D.C. Rees Structure of the Escherichia coli fumarate reductase respiratory complex Science 284 1999 1961 1966
    • (1999) Science , vol.284 , pp. 1961-1966
    • Iverson, T.M.1    Luna-Chavez, C.2    Cecchini, G.3    Rees, D.C.4
  • 20
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 1991 110 119
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 21
    • 0010049951 scopus 로고    scopus 로고
    • Structure of fumarate reductase from Wolinella succinogenes at 2.2 a resolution
    • C.R. Lancaster, A. Kroger, M. Auer, and H. Michel Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution Nature 402 1999 377 385
    • (1999) Nature , vol.402 , pp. 377-385
    • Lancaster, C.R.1    Kroger, A.2    Auer, M.3    Michel, H.4
  • 22
    • 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
  • 24
    • 0001442551 scopus 로고
    • Identification of the ubiquinone-binding domain in QPs1 of succinate-ubiquinone reductase
    • G.Y. Lee, D.Y. He, L. Yu, and C.A. Yu Identification of the ubiquinone-binding domain in QPs1 of succinate-ubiquinone reductase J. Biol. Chem. 270 1995 6193 6198
    • (1995) J. Biol. Chem. , vol.270 , pp. 6193-6198
    • Lee, G.Y.1    He, D.Y.2    Yu, L.3    Yu, C.A.4
  • 25
    • 0037122944 scopus 로고    scopus 로고
    • Quinol:fumarate oxidoreductases and succinate:quinone oxidoreductases: Phylogenetic relationships, metal centres and membrane attachment
    • R.S. Lemos, A.S. Fernandes, M.M. Pereira, C.M. Gomes, and M. Teixeira Quinol:fumarate oxidoreductases and succinate:quinone oxidoreductases: phylogenetic relationships, metal centres and membrane attachment Biochim. Biophys. Acta 1553 2002 158 170
    • (2002) Biochim. Biophys. Acta , vol.1553 , pp. 158-170
    • Lemos, R.S.1    Fernandes, A.S.2    Pereira, M.M.3    Gomes, C.M.4    Teixeira, M.5
  • 26
    • 0034479757 scopus 로고    scopus 로고
    • A new method for Protein Structure Comparisons and Similarity Searches
    • G. Lu A new method for Protein Structure Comparisons and Similarity Searches J. Appl. Crystallogr. 33 2000 176 183
    • (2000) J. Appl. Crystallogr. , vol.33 , pp. 176-183
    • Lu, G.1
  • 27
    • 0033568501 scopus 로고    scopus 로고
    • Comparison of catalytic activity and inhibitors of quinone reactions of succinate dehydrogenase (Succinate-ubiquinone oxidoreductase) and fumarate reductase (Menaquinol-fumarate oxidoreductase) from Escherichia coli
    • E. Maklashina, and G. Cecchini Comparison of catalytic activity and inhibitors of quinone reactions of succinate dehydrogenase (Succinate-ubiquinone oxidoreductase) and fumarate reductase (Menaquinol-fumarate oxidoreductase) from Escherichia coli Arch. Biochem. Biophys. 369 1999 223 232
    • (1999) Arch. Biochem. Biophys. , vol.369 , pp. 223-232
    • Maklashina, E.1    Cecchini, G.2
  • 29
    • 0037044847 scopus 로고    scopus 로고
    • Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase
    • K.R. Messner, and J.A. Imlay Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase J. Biol. Chem. 277 2002 42563 42571
    • (2002) J. Biol. Chem. , vol.277 , pp. 42563-42571
    • Messner, K.R.1    Imlay, J.A.2
  • 30
    • 0026601555 scopus 로고
    • Characterization of ubisemiquinone radicals in succinate-ubiquinone reductase
    • T. Miki, L. Yu, and C.A. Yu Characterization of ubisemiquinone radicals in succinate-ubiquinone reductase Arch. Biochem. Biophys. 293 1992 61 66
    • (1992) Arch. Biochem. Biophys. , vol.293 , pp. 61-66
    • Miki, T.1    Yu, L.2    Yu, C.A.3
  • 31
    • 0035874016 scopus 로고    scopus 로고
    • Novel mutations and the emergence of a common mutation in the SDHD gene causing familial paraganglioma
    • J.M. Milunsky, T.A. Maher, V.V. Michels, and A. Milunsky Novel mutations and the emergence of a common mutation in the SDHD gene causing familial paraganglioma Am. J. Med. Genet. 100 2001 311 314
    • (2001) Am. J. Med. Genet. , vol.100 , pp. 311-314
    • Milunsky, J.M.1    Maher, T.A.2    Michels, V.V.3    Milunsky, A.4
  • 33
    • 0033767445 scopus 로고    scopus 로고
    • Mutations in SDHC cause autosomal dominant paraganglioma, type 3
    • S. Niemann, and U. Muller Mutations in SDHC cause autosomal dominant paraganglioma, type 3 Nat. Genet. 26 2000 268 270
    • (2000) Nat. Genet. , vol.26 , pp. 268-270
    • Niemann, S.1    Muller, U.2
  • 34
    • 0018971809 scopus 로고
    • Differential effects of antimycin on ubisemiquinone bound in different environments in isolated succinate. cytochrome c reductase complex
    • T. Ohnishi, and B.L. Trumpower Differential effects of antimycin on ubisemiquinone bound in different environments in isolated succinate. cytochrome c reductase complex J. Biol. Chem. 255 1980 3278 3284
    • (1980) J. Biol. Chem. , vol.255 , pp. 3278-3284
    • Ohnishi, T.1    Trumpower, B.L.2
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W. Carter Jr. R.M. Sweet Academic Press New York
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode C.W. Carter Jr. R.M. Sweet Macromolecular Crystallography, Part A 1997 Academic Press New York 307 326
    • (1997) Macromolecular Crystallography, Part a , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0033588181 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase. Identification of Sdh3p amino acid residues involved in ubiquinone binding
    • K.S. Oyedotun, and B.D. Lemire The Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase. Identification of Sdh3p amino acid residues involved in ubiquinone binding J. Biol. Chem. 274 1999 23956 23962
    • (1999) J. Biol. Chem. , vol.274 , pp. 23956-23962
    • Oyedotun, K.S.1    Lemire, B.D.2
  • 37
    • 0035907323 scopus 로고    scopus 로고
    • The Quinone-binding sites of the Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase
    • K.S. Oyedotun, and B.D. Lemire The Quinone-binding sites of the Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase J. Biol. Chem. 276 2001 16936 16943
    • (2001) J. Biol. Chem. , vol.276 , pp. 16936-16943
    • Oyedotun, K.S.1    Lemire, B.D.2
  • 38
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • C.C. Page, C.C. Moser, X. Chen, and P.L. Dutton Natural engineering principles of electron tunnelling in biological oxidation-reduction Nature 402 1999 47 52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 39
    • 0034059135 scopus 로고    scopus 로고
    • Compound heterozygous mutations in the flavoprotein gene of the respiratory chain complex II in a patient with Leigh syndrome
    • B. Parfait, D. Chretien, A. Rotig, C. Marsac, A. Munnich, and P. Rustin Compound heterozygous mutations in the flavoprotein gene of the respiratory chain complex II in a patient with Leigh syndrome Hum. Genet. 106 2000 236 243
    • (2000) Hum. Genet. , vol.106 , pp. 236-243
    • Parfait, B.1    Chretien, D.2    Rotig, A.3    Marsac, C.4    Munnich, A.5    Rustin, P.6
  • 40
    • 0037122936 scopus 로고    scopus 로고
    • Inborn errors of complex II - Unusual human mitochondrial diseases
    • P. Rustin, and A. Rotig Inborn errors of complex II - unusual human mitochondrial diseases Biochim. Biophys. Acta 1553 2002 117 122
    • (2002) Biochim. Biophys. Acta , vol.1553 , pp. 117-122
    • Rustin, P.1    Rotig, A.2
  • 42
    • 0017753193 scopus 로고
    • A transmembrane quinone pair in the succinate dehydrogenase - Cytochrome b region
    • J.C. Salerno, H.J. Harmon, H. Blum, J.S. Leigh, and T. Ohnishi A transmembrane quinone pair in the succinate dehydrogenase - cytochrome b region FEBS Lett. 82 1977 179 182
    • (1977) FEBS Lett. , vol.82 , pp. 179-182
    • Salerno, J.C.1    Harmon, H.J.2    Blum, H.3    Leigh, J.S.4    Ohnishi, T.5
  • 43
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siecle
    • M. Saraste Oxidative phosphorylation at the fin de siecle Science 283 1999 1488 1493
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 44
    • 0030841921 scopus 로고    scopus 로고
    • The smallest membrane anchoring subunit (QPs3) of bovine heart mitochondrial succinate-ubiquinone reductase. Cloning, sequencing, topology, and Q-binding domain
    • S.K. Shenoy, L. Yu, and C.A. Yu The smallest membrane anchoring subunit (QPs3) of bovine heart mitochondrial succinate-ubiquinone reductase. Cloning, sequencing, topology, and Q-binding domain J. Biol. Chem. 272 1997 17867 17872
    • (1997) J. Biol. Chem. , vol.272 , pp. 17867-17872
    • Shenoy, S.K.1    Yu, L.2    Yu, C.A.3
  • 45
    • 0033605579 scopus 로고    scopus 로고
    • Identification of quinone-binding and heme-ligating residues of the smallest membrane-anchoring subunit (QPs3) of bovine heart mitochondrial succinate:ubiquinone reductase
    • S.K. Shenoy, L. Yu, and C. Yu Identification of quinone-binding and heme-ligating residues of the smallest membrane-anchoring subunit (QPs3) of bovine heart mitochondrial succinate:ubiquinone reductase J. Biol. Chem. 274 1999 8717 8722
    • (1999) J. Biol. Chem. , vol.274 , pp. 8717-8722
    • Shenoy, S.K.1    Yu, L.2    Yu, C.3
  • 48
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 53
    • 0023217485 scopus 로고
    • Stabilized ubisemiquinone in reconstituted succinate ubiquinone reductase
    • Y. Xu, J.C. Salerno, Y.H. Wei, and T.E. King Stabilized ubisemiquinone in reconstituted succinate ubiquinone reductase Biochem. Biophys. Res. Commun. 144 1987 315 322
    • (1987) Biochem. Biophys. Res. Commun. , vol.144 , pp. 315-322
    • Xu, Y.1    Salerno, J.C.2    Wei, Y.H.3    King, T.E.4
  • 54
    • 0029787270 scopus 로고    scopus 로고
    • Inhibitor probes of the quinone binding sites of mammalian complex II and Escherichia coli fumarate reductase
    • V. Yankovskaya, S.O. Sablin, R.R. Ramsay, T.P. Singer, B.A. Ackrell, G. Cecchini, and H. Miyoshi Inhibitor probes of the quinone binding sites of mammalian complex II and Escherichia coli fumarate reductase J. Biol. Chem. 271 1996 21020 21024
    • (1996) J. Biol. Chem. , vol.271 , pp. 21020-21024
    • Yankovskaya, V.1    Sablin, S.O.2    Ramsay, R.R.3    Singer, T.P.4    Ackrell, B.A.5    Cecchini, G.6    Miyoshi, H.7
  • 56
    • 0023153684 scopus 로고
    • Properties of bovine heart mitochondrial cytochrome b560
    • L. Yu, J.X. Xu, P.E. Haley, and C.A. Yu Properties of bovine heart mitochondrial cytochrome b560 J. Biol. Chem. 262 1987 1137 1143
    • (1987) J. Biol. Chem. , vol.262 , pp. 1137-1143
    • Yu, L.1    Xu, J.X.2    Haley, P.E.3    Yu, C.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.