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Volumn 1857, Issue 7, 2016, Pages 872-883

Energy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex i

Author keywords

Electron paramagnetic resonance; Iron sulfur cluster; NADH:ubiquinone oxidoreductase; Proton coupled electron transfer; Semiquinone; Superoxide

Indexed keywords

FLAVINE MONONUCLEOTIDE; IRON SULFUR PROTEIN; NITRATE REDUCTASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SEMIQUINONE; SUPEROXIDE; UBIQUINOL CYTOCHROME C REDUCTASE; UBIQUINONE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PROTEIN BINDING;

EID: 84955588367     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2015.12.009     Document Type: Article
Times cited : (110)

References (104)
  • 1
    • 84878905186 scopus 로고    scopus 로고
    • Mitochondrial complex i
    • J. Hirst Mitochondrial complex I Annu. Rev. Biochem. 82 2013 551 575
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 551-575
    • Hirst, J.1
  • 2
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • M.P. Murphy How mitochondria produce reactive oxygen species Biochem. J. 417 2009 1 13
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 3
    • 84870266832 scopus 로고    scopus 로고
    • Complex i deficiency: Clinical features, biochemistry and molecular genetics
    • E. Fassone, and S. Rahman Complex I deficiency: clinical features, biochemistry and molecular genetics J. Med. Genet. 49 2012 578 590
    • (2012) J. Med. Genet. , vol.49 , pp. 578-590
    • Fassone, E.1    Rahman, S.2
  • 5
    • 84915761829 scopus 로고    scopus 로고
    • Architecture of mammalian complex i
    • K.R. Vinothkumar, J. Zhu, and J. Hirst Architecture of mammalian complex I Nature 515 2014 80 84
    • (2014) Nature , vol.515 , pp. 80-84
    • Vinothkumar, K.R.1    Zhu, J.2    Hirst, J.3
  • 6
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • J.E. Walker The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains Q. Rev. Biophys. 25 1992 253 324
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 8
    • 79959731297 scopus 로고    scopus 로고
    • Why does mitochondrial complex i have so many subunits?
    • J. Hirst Why does mitochondrial complex I have so many subunits? Biochem. J. 437 2011 e1 e3
    • (2011) Biochem. J. , vol.437 , pp. e1-e3
    • Hirst, J.1
  • 9
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex i from Thermus thermophilus
    • L.A. Sazanov, and P. Hinchliffe Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus Science 311 2006 1430 1436
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 10
    • 80052068980 scopus 로고    scopus 로고
    • Structure of the membrane domain of respiratory complex i
    • R.G. Efremov, and L.A. Sazanov Structure of the membrane domain of respiratory complex I Nature 476 2011 414 420
    • (2011) Nature , vol.476 , pp. 414-420
    • Efremov, R.G.1    Sazanov, L.A.2
  • 11
  • 13
    • 84886551592 scopus 로고    scopus 로고
    • Investigating the function of [2Fe-2S] cluster N1a, the off-pathway cluster in complex I, by manipulating its reduction potential
    • J.A. Birrell, K. Morina, H.R. Bridges, T. Friedrich, and J. Hirst Investigating the function of [2Fe-2S] cluster N1a, the off-pathway cluster in complex I, by manipulating its reduction potential Biochem. J. 456 2013 139 146
    • (2013) Biochem. J. , vol.456 , pp. 139-146
    • Birrell, J.A.1    Morina, K.2    Bridges, H.R.3    Friedrich, T.4    Hirst, J.5
  • 15
    • 0037613548 scopus 로고    scopus 로고
    • + by the catalytic (Iλ) subcomplex of mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • + by the catalytic (Iλ) subcomplex of mitochondrial NADH:ubiquinone oxidoreductase (complex I) J. Am. Chem. Soc. 125 2003 6020 6021
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6020-6021
    • Zu, Y.1    Shannon, R.J.2    Hirst, J.3
  • 16
    • 70350351403 scopus 로고    scopus 로고
    • Structural basis for the mechanism of respiratory complex i
    • J.M. Berrisford, and L.A. Sazanov Structural basis for the mechanism of respiratory complex I J. Biol. Chem. 284 2009 29773 29783
    • (2009) J. Biol. Chem. , vol.284 , pp. 29773-29783
    • Berrisford, J.M.1    Sazanov, L.A.2
  • 17
    • 0034161331 scopus 로고    scopus 로고
    • Flavoenzymes: Diverse catalysts with recurrent features
    • M.W. Fraaije, and A. Mattevi Flavoenzymes: diverse catalysts with recurrent features Trends Biochem. Sci. 25 2000 126 132
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 126-132
    • Fraaije, M.W.1    Mattevi, A.2
  • 18
    • 84878930284 scopus 로고    scopus 로고
    • + dissociation during NADH oxidation by mitochondrial complex i using modified nicotinamide nucleotides
    • + dissociation during NADH oxidation by mitochondrial complex I using modified nicotinamide nucleotides Biochemistry 52 2013 4048 4055
    • (2013) Biochemistry , vol.52 , pp. 4048-4055
    • Birrell, J.A.1    Hirst, J.2
  • 19
    • 79960383683 scopus 로고    scopus 로고
    • A ternary mechanism for NADH oxidation by positively charged electron acceptors, catalyzed at the flavin site in respiratory complex i
    • J.A. Birrell, M.S. King, and J. Hirst A ternary mechanism for NADH oxidation by positively charged electron acceptors, catalyzed at the flavin site in respiratory complex I FEBS Lett. 585 2011 2318 2322
    • (2011) FEBS Lett. , vol.585 , pp. 2318-2322
    • Birrell, J.A.1    King, M.S.2    Hirst, J.3
  • 20
    • 17144366976 scopus 로고    scopus 로고
    • Generation of superoxide-radical by the NADH:ubiquinone oxidoreductase of heart mitochondria
    • A.D. Vinogradov, and V.G. Grivennikova Generation of superoxide-radical by the NADH:ubiquinone oxidoreductase of heart mitochondria Biochem. Mosc. 70 2005 120 127
    • (2005) Biochem. Mosc. , vol.70 , pp. 120-127
    • Vinogradov, A.D.1    Grivennikova, V.G.2
  • 21
    • 84958766908 scopus 로고    scopus 로고
    • A self-assembled respiratory chain that catalyzes NADH oxidation by ubiquinone-10 cycling between complex i and the alternative oxidase
    • A.J.Y. Jones, J.N. Blaza, H.R. Bridges, B. May, A.L. Moore, and J. Hirst A self-assembled respiratory chain that catalyzes NADH oxidation by ubiquinone-10 cycling between complex I and the alternative oxidase Angew. Chem. Int. Ed. Engl. 55 2016 728 731
    • (2016) Angew. Chem. Int. Ed. Engl. , vol.55 , pp. 728-731
    • Jones, A.J.Y.1    Blaza, J.N.2    Bridges, H.R.3    May, B.4    Moore, A.L.5    Hirst, J.6
  • 22
    • 80052154091 scopus 로고    scopus 로고
    • Reversibility and efficiency in electrocatalytic energy conversion and lessons from enzymes
    • F.A. Armstrong, and J. Hirst Reversibility and efficiency in electrocatalytic energy conversion and lessons from enzymes Proc. Natl. Acad. Sci. U. S. A. 108 2011 14049 14054
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 14049-14054
    • Armstrong, F.A.1    Hirst, J.2
  • 23
    • 79955977892 scopus 로고    scopus 로고
    • Superoxide is produced by the reduced flavin in mitochondrial complex I: A single, unified mechanism that applies during both forward and reverse electron transfer
    • K.R. Pryde, and J. Hirst Superoxide is produced by the reduced flavin in mitochondrial complex I: a single, unified mechanism that applies during both forward and reverse electron transfer J. Biol. Chem. 286 2011 18056 18065
    • (2011) J. Biol. Chem. , vol.286 , pp. 18056-18065
    • Pryde, K.R.1    Hirst, J.2
  • 24
    • 0027990677 scopus 로고
    • Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • V.D. Sled, N.I. Rudnitzky, Y. Hatefi, and T. Ohnishi Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I) Biochemistry 33 1994 10069 10075
    • (1994) Biochemistry , vol.33 , pp. 10069-10075
    • Sled, V.D.1    Rudnitzky, N.I.2    Hatefi, Y.3    Ohnishi, T.4
  • 25
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    • L. Kussmaul, and J. Hirst The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria Proc. Natl. Acad. Sci. U. S. A. 103 2006 7607 7612
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 27
    • 0032490089 scopus 로고    scopus 로고
    • Iron-sulfur clusters/semiquinones in complex i
    • T. Ohnishi Iron-sulfur clusters/semiquinones in complex I Biochim. Biophys. Acta 1364 1998 186 206
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 186-206
    • Ohnishi, T.1
  • 28
    • 0020494651 scopus 로고
    • New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria
    • H. Beinert, and S.P.J. Albracht New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria Biochim. Biophys. Acta 683 1982 245 277
    • (1982) Biochim. Biophys. Acta , vol.683 , pp. 245-277
    • Beinert, H.1    Albracht, S.P.J.2
  • 29
    • 0002727146 scopus 로고
    • Mitochondrial iron-sulfur flavodehydrogenases
    • R. Capaldi, Marcel Dekker New York
    • T. Ohnishi Mitochondrial iron-sulfur flavodehydrogenases R. Capaldi, Membrane Proteins in Energy Transduction 1979 Marcel Dekker New York 1 87
    • (1979) Membrane Proteins in Energy Transduction , pp. 1-87
    • Ohnishi, T.1
  • 30
    • 34547917597 scopus 로고    scopus 로고
    • Reevaluating the relationship between EPR spectra and enzyme structure for the iron-sulfur clusters in NADH:quinone oxidoreductase
    • G. Yakovlev, T. Reda, and J. Hirst Reevaluating the relationship between EPR spectra and enzyme structure for the iron-sulfur clusters in NADH:quinone oxidoreductase Proc. Natl. Acad. Sci. U. S. A. 104 2007 12720 12725
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 12720-12725
    • Yakovlev, G.1    Reda, T.2    Hirst, J.3
  • 31
    • 76649102458 scopus 로고    scopus 로고
    • Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex i by double electron-electron resonance
    • M.M. Roessler, M.S. King, A.J. Robinson, F.A. Armstrong, J. Harmer, and J. Hirst Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron-electron resonance Proc. Natl. Acad. Sci. U. S. A. 107 2010 1930 1935
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 1930-1935
    • Roessler, M.M.1    King, M.S.2    Robinson, A.J.3    Armstrong, F.A.4    Harmer, J.5    Hirst, J.6
  • 32
    • 0019324533 scopus 로고
    • An analysis of some thermodynamic properties of iron-sulphur centres in site i of mitochondria
    • W.J. Ingledew, and T. Ohnishi An analysis of some thermodynamic properties of iron-sulphur centres in site I of mitochondria Biochem. J. 186 1980 111 117
    • (1980) Biochem. J. , vol.186 , pp. 111-117
    • Ingledew, W.J.1    Ohnishi, T.2
  • 34
    • 84856917379 scopus 로고    scopus 로고
    • Mössbauer spectroscopy on respiratory complex I: The iron-sulfur cluster ensemble in the NADH-reduced enzyme is partially oxidized
    • H.R. Bridges, E. Bill, and J. Hirst Mössbauer spectroscopy on respiratory complex I: the iron-sulfur cluster ensemble in the NADH-reduced enzyme is partially oxidized Biochemistry 51 2012 149 158
    • (2012) Biochemistry , vol.51 , pp. 149-158
    • Bridges, H.R.1    Bill, E.2    Hirst, J.3
  • 36
    • 84923084767 scopus 로고    scopus 로고
    • Electron tunneling rates in respiratory complex i are tuned for efficient energy conversion
    • S. de Vries, K. Dörner, M.J.F. Strampraad, and T. Friedrich Electron tunneling rates in respiratory complex I are tuned for efficient energy conversion Angew. Chem. Int. Ed. 54 2015 2844 2848
    • (2015) Angew. Chem. Int. Ed. , vol.54 , pp. 2844-2848
    • De Vries, S.1    Dörner, K.2    Strampraad, M.J.F.3    Friedrich, T.4
  • 37
    • 84874101282 scopus 로고    scopus 로고
    • Principles of sustained enzymatic hydrogen oxidation in the presence of oxygen - The crucial influence of high potential Fe-S clusters in the electron relay of [NiFe]-hydrogenases
    • R.M. Evans, A. Parkin, M.M. Roessler, B.J. Murphy, H. Adamson, M.J. Lukey, F. Sargent, A. Volbeda, J.C. Fontecilla-Camps, and F.A. Armstrong Principles of sustained enzymatic hydrogen oxidation in the presence of oxygen - the crucial influence of high potential Fe-S clusters in the electron relay of [NiFe]-hydrogenases J. Am. Chem. Soc. 135 2013 2694 2707
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 2694-2707
    • Evans, R.M.1    Parkin, A.2    Roessler, M.M.3    Murphy, B.J.4    Adamson, H.5    Lukey, M.J.6    Sargent, F.7    Volbeda, A.8    Fontecilla-Camps, J.C.9    Armstrong, F.A.10
  • 38
    • 79955027963 scopus 로고    scopus 로고
    • Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus
    • M.-E. Pandelia, W. Nitschke, P. Infossi, M.-T. Giudici-Orticoni, E. Bill, and W. Lubitz Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus Proc. Natl. Acad. Sci. U. S. A. 108 2011 6097 6102
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 6097-6102
    • Pandelia, M.-E.1    Nitschke, W.2    Infossi, P.3    Giudici-Orticoni, M.-T.4    Bill, E.5    Lubitz, W.6
  • 39
    • 80855156729 scopus 로고    scopus 로고
    • Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase
    • Y. Shomura, K.S. Yoon, H. Nishihara, and Y. Higuchi Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase Nature 479 2011 253 256
    • (2011) Nature , vol.479 , pp. 253-256
    • Shomura, Y.1    Yoon, K.S.2    Nishihara, H.3    Higuchi, Y.4
  • 40
    • 84866518261 scopus 로고    scopus 로고
    • 2-tolerant [NiFe]-hydrogenase Hyd-1 from Escherichia coli and characterization of the unique [4Fe-3S] cluster by HYSCORE
    • 2-tolerant [NiFe]-hydrogenase Hyd-1 from Escherichia coli and characterization of the unique [4Fe-3S] cluster by HYSCORE J. Am. Chem. Soc. 134 2012 15581 15594
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 15581-15594
    • Roessler, M.M.1    Evans, R.M.2    Davies, R.A.3    Harmer, J.4    Armstrong, F.A.5
  • 42
    • 33847687662 scopus 로고    scopus 로고
    • Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain
    • L.A. Sazanov Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain Biochemistry 46 2007 2275 2288
    • (2007) Biochemistry , vol.46 , pp. 2275-2288
    • Sazanov, L.A.1
  • 43
    • 41149100550 scopus 로고    scopus 로고
    • Production of reactive oxygen species by complex i (NADH:ubiquinone oxidoreductase) from Escherichia coli and comparison to the enzyme from mitochondria
    • D. Esterházy, M.S. King, G. Yakovlev, and J. Hirst Production of reactive oxygen species by complex I (NADH:ubiquinone oxidoreductase) from Escherichia coli and comparison to the enzyme from mitochondria Biochemistry 47 2008 3964 3971
    • (2008) Biochemistry , vol.47 , pp. 3964-3971
    • Esterházy, D.1    King, M.S.2    Yakovlev, G.3    Hirst, J.4
  • 44
    • 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
  • 45
    • 0029075136 scopus 로고
    • Isolation and characterization of the proton-translocating NADH:ubiquinone oxidoreductase from Escherichia coli
    • H. Leif, V.D. Sled, T. Ohnishi, H. Weiss, and T. Friedrich Isolation and characterization of the proton-translocating NADH:ubiquinone oxidoreductase from Escherichia coli Eur. J. Biochem. 230 1995 538 548
    • (1995) Eur. J. Biochem. , vol.230 , pp. 538-548
    • Leif, H.1    Sled, V.D.2    Ohnishi, T.3    Weiss, H.4    Friedrich, T.5
  • 46
    • 0025091989 scopus 로고
    • Studies on the NADH-menaquinone oxidoreductase segment of the respiratory chain in Thermus thermophilus HB-8
    • S.W. Meinhardt, D.C. Wang, K. Hon-nami, T. Yagi, T. Oshima, and T. Ohnishi Studies on the NADH-menaquinone oxidoreductase segment of the respiratory chain in Thermus thermophilus HB-8 J. Biol. Chem. 265 1990 1360 1368
    • (1990) J. Biol. Chem. , vol.265 , pp. 1360-1368
    • Meinhardt, S.W.1    Wang, D.C.2    Hon-Nami, K.3    Yagi, T.4    Oshima, T.5    Ohnishi, T.6
  • 47
    • 33645655818 scopus 로고    scopus 로고
    • Identification of a novel subunit of respiratory complex i from Thermus thermophilus
    • P. Hinchliffe, J. Carroll, and L.A. Sazanov Identification of a novel subunit of respiratory complex I from Thermus thermophilus Biochemistry 45 2006 4413 4420
    • (2006) Biochemistry , vol.45 , pp. 4413-4420
    • Hinchliffe, P.1    Carroll, J.2    Sazanov, L.A.3
  • 48
    • 33748985025 scopus 로고    scopus 로고
    • The menaquinol-oxidizing cytochrome bc complex from Thermus thermophilus: Protein domains and subunits
    • D. Mooser, O. Maneg, F. MacMillan, F. Malatesta, T. Soulimane, and B. Ludwig The menaquinol-oxidizing cytochrome bc complex from Thermus thermophilus: protein domains and subunits Biochim. Biophys. Acta 1757 2006 1084 1095
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1084-1095
    • Mooser, D.1    Maneg, O.2    MacMillan, F.3    Malatesta, F.4    Soulimane, T.5    Ludwig, B.6
  • 49
    • 0021144978 scopus 로고
    • The respiratory chains of Escherichia coli
    • W.J. Ingledew, and R.K. Poole The respiratory chains of Escherichia coli Microbiol. Rev. 48 1984 222 271
    • (1984) Microbiol. Rev. , vol.48 , pp. 222-271
    • Ingledew, W.J.1    Poole, R.K.2
  • 50
    • 84883159462 scopus 로고    scopus 로고
    • Post-translational modifications near the quinone binding site of mammalian complex i
    • J. Carroll, S. Ding, I.M. Fearnley, and J.E. Walker Post-translational modifications near the quinone binding site of mammalian complex I J. Biol. Chem. 288 2013 24799 24808
    • (2013) J. Biol. Chem. , vol.288 , pp. 24799-24808
    • Carroll, J.1    Ding, S.2    Fearnley, I.M.3    Walker, J.E.4
  • 52
    • 84898969936 scopus 로고    scopus 로고
    • 4] proteins involved in isoprenoid biosynthesis
    • 4] proteins involved in isoprenoid biosynthesis Angew. Chem. Int. Ed. 53 2014 4294 4310
    • (2014) Angew. Chem. Int. Ed. , vol.53 , pp. 4294-4310
    • Wang, W.1    Oldfield, E.2
  • 53
    • 33747370385 scopus 로고    scopus 로고
    • The redox-Bohr group associated with iron-sulfur cluster N2 of complex i
    • K. Zwicker, A. Galkin, S. Dröse, L. Grgic, S. Kerscher, and U. Brandt The redox-Bohr group associated with iron-sulfur cluster N2 of complex I J. Biol. Chem. 281 2006 23013 23017
    • (2006) J. Biol. Chem. , vol.281 , pp. 23013-23017
    • Zwicker, K.1    Galkin, A.2    Dröse, S.3    Grgic, L.4    Kerscher, S.5    Brandt, U.6
  • 54
    • 2442701768 scopus 로고    scopus 로고
    • Functional significance of conserved histidines and arginines in the 49-kDa subunit of mitochondrial complex i
    • L. Grgic, K. Zwicker, N. Kashani-Poor, S. Kerscher, and U. Brandt Functional significance of conserved histidines and arginines in the 49-kDa subunit of mitochondrial complex I J. Biol. Chem. 279 2004 21193 21199
    • (2004) J. Biol. Chem. , vol.279 , pp. 21193-21199
    • Grgic, L.1    Zwicker, K.2    Kashani-Poor, N.3    Kerscher, S.4    Brandt, U.5
  • 59
    • 51049093616 scopus 로고    scopus 로고
    • Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex i
    • A. Galkin, B. Meyer, I. Wittig, M. Karas, H. Schägger, A. Vinogradov, and U. Brandt Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex I J. Biol. Chem. 283 2008 20907 20913
    • (2008) J. Biol. Chem. , vol.283 , pp. 20907-20913
    • Galkin, A.1    Meyer, B.2    Wittig, I.3    Karas, M.4    Schägger, H.5    Vinogradov, A.6    Brandt, U.7
  • 60
    • 84890282866 scopus 로고    scopus 로고
    • Oxidoreduction properties of bound ubiquinone in complex i from Escherichia coli
    • M. Verkhovskaya, and M. Wikström Oxidoreduction properties of bound ubiquinone in complex I from Escherichia coli Biochim. Biophys. Acta 1837 2014 246 250
    • (2014) Biochim. Biophys. Acta , vol.1837 , pp. 246-250
    • Verkhovskaya, M.1    Wikström, M.2
  • 61
    • 84864659415 scopus 로고    scopus 로고
    • The coupling mechanism of respiratory complex i - A structural and evolutionary perspective
    • R.G. Efremov, and L.A. Sazanov The coupling mechanism of respiratory complex I - a structural and evolutionary perspective Biochim. Biophys. Acta 1817 2012 1785 1795
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1785-1795
    • Efremov, R.G.1    Sazanov, L.A.2
  • 62
    • 84918561145 scopus 로고    scopus 로고
    • Pinpoint chemical modification of Asp160 in the 49 kDa subunit of bovine mitochondrial complex i via a combination of ligand-directed tosyl chemistry and click chemistry
    • T. Masuya, M. Murai, H. Morisaka, and H. Miyoshi Pinpoint chemical modification of Asp160 in the 49 kDa subunit of bovine mitochondrial complex I via a combination of ligand-directed tosyl chemistry and click chemistry Biochemistry 53 2014 7816 7823
    • (2014) Biochemistry , vol.53 , pp. 7816-7823
    • Masuya, T.1    Murai, M.2    Morisaka, H.3    Miyoshi, H.4
  • 63
    • 84928944969 scopus 로고    scopus 로고
    • Amilorides bind to the quinone binding pocket of bovine mitochondrial complex i
    • M. Murai, S. Murakami, T. Ito, and H. Miyoshi Amilorides bind to the quinone binding pocket of bovine mitochondrial complex I Biochemistry 54 2015 2739 2746
    • (2015) Biochemistry , vol.54 , pp. 2739-2746
    • Murai, M.1    Murakami, S.2    Ito, T.3    Miyoshi, H.4
  • 64
  • 65
    • 84890493866 scopus 로고    scopus 로고
    • Characterization of two quinone radicals in the NADH:ubiquinone oxidoreductase from Escherichia coli by a combined fluorescence spectroscopic and electrochemical approach
    • R. Hielscher, M. Yegres, M. Voicescu, E. Gnandt, T. Friedrich, and P. Hellwig Characterization of two quinone radicals in the NADH:ubiquinone oxidoreductase from Escherichia coli by a combined fluorescence spectroscopic and electrochemical approach Biochemistry 52 2013 8993 9000
    • (2013) Biochemistry , vol.52 , pp. 8993-9000
    • Hielscher, R.1    Yegres, M.2    Voicescu, M.3    Gnandt, E.4    Friedrich, T.5    Hellwig, P.6
  • 66
    • 80051601805 scopus 로고    scopus 로고
    • A two-state stabilization-change mechanism for proton-pumping complex i
    • U. Brandt A two-state stabilization-change mechanism for proton-pumping complex I Biochim. Biophys. Acta 1807 2011 1364 1369
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1364-1369
    • Brandt, U.1
  • 67
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron-proton transfer
    • M.H. Stowell, T.M. McPhillips, D.C. Rees, S.M. Soltis, E. Abresch, and G. Feher Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer Science 276 1997 812 816
    • (1997) Science , vol.276 , pp. 812-816
    • Stowell, M.H.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 71
    • 13444259531 scopus 로고    scopus 로고
    • Nf) and the interaction with cluster N2: New insight into the energy-coupled electron transfer in complex i
    • Nf) and the interaction with cluster N2: new insight into the energy-coupled electron transfer in complex I Biochemistry 44 2005 1744 1754
    • (2005) Biochemistry , vol.44 , pp. 1744-1754
    • Yano, T.1    Dunham, W.R.2    Ohnishi, T.3
  • 78
    • 0017406503 scopus 로고
    • Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
    • E. Cadenas, A. Boveris, C.I. Ragan, and A.O. Stoppani Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria Arch. Biochem. Biophys. 180 1977 248 257
    • (1977) Arch. Biochem. Biophys. , vol.180 , pp. 248-257
    • Cadenas, E.1    Boveris, A.2    Ragan, C.I.3    Stoppani, A.O.4
  • 79
    • 79961008706 scopus 로고    scopus 로고
    • Evidence for two sites of superoxide production by mitochondrial NADH-ubiquinone oxidoreductase (complex I)
    • J.R. Treberg, C.L. Quinlan, and M.D. Brand Evidence for two sites of superoxide production by mitochondrial NADH-ubiquinone oxidoreductase (complex I) J. Biol. Chem. 286 2011 27103 27110
    • (2011) J. Biol. Chem. , vol.286 , pp. 27103-27110
    • Treberg, J.R.1    Quinlan, C.L.2    Brand, M.D.3
  • 80
    • 53849099653 scopus 로고    scopus 로고
    • The production of reactive oxygen species by complex i
    • J. Hirst, M.S. King, and K.R. Pryde The production of reactive oxygen species by complex I Biochem. Soc. Trans. 36 2008 976 980
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 976-980
    • Hirst, J.1    King, M.S.2    Pryde, K.R.3
  • 81
    • 4544354262 scopus 로고    scopus 로고
    • Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • A.J. Lambert, and M.D. Brand Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I) J. Biol. Chem. 279 2004 39414 39420
    • (2004) J. Biol. Chem. , vol.279 , pp. 39414-39420
    • Lambert, A.J.1    Brand, M.D.2
  • 82
    • 4043090717 scopus 로고    scopus 로고
    • Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane
    • A.J. Lambert, and M.D. Brand Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane Biochem. J. 382 2004 511 517
    • (2004) Biochem. J. , vol.382 , pp. 511-517
    • Lambert, A.J.1    Brand, M.D.2
  • 84
    • 64549096768 scopus 로고    scopus 로고
    • Reduction of hydrophilic ubiquinones by the flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I) and production of reactive oxygen species
    • M.S. King, M.S. Sharpley, and J. Hirst Reduction of hydrophilic ubiquinones by the flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I) and production of reactive oxygen species Biochemistry 48 2009 2053 2062
    • (2009) Biochemistry , vol.48 , pp. 2053-2062
    • King, M.S.1    Sharpley, M.S.2    Hirst, J.3
  • 85
    • 84883180274 scopus 로고    scopus 로고
    • Energy transducing roles of antiporter-like subunits in Escherichia coli NDH-1 with main focus on subunit NuoN (ND2)
    • M. Sato, P.K. Sinha, J. Torres-Bacete, A. Matsuno-Yagi, and T. Yagi Energy transducing roles of antiporter-like subunits in Escherichia coli NDH-1 with main focus on subunit NuoN (ND2) J. Biol. Chem. 288 2013 24705 24716
    • (2013) J. Biol. Chem. , vol.288 , pp. 24705-24716
    • Sato, M.1    Sinha, P.K.2    Torres-Bacete, J.3    Matsuno-Yagi, A.4    Yagi, T.5
  • 87
    • 84863220590 scopus 로고    scopus 로고
    • Tightly-bound ubiquinone in the Escherichia coli respiratory complex i
    • M. Verkhovsky, D.A. Bloch, and M. Verkhovskaya Tightly-bound ubiquinone in the Escherichia coli respiratory complex I Biochim. Biophys. Acta 1817 2012 1550 1556
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1550-1556
    • Verkhovsky, M.1    Bloch, D.A.2    Verkhovskaya, M.3
  • 89
    • 11844287666 scopus 로고    scopus 로고
    • Thermodynamic and EPR studies of slowly relaxing ubisemiquinone species in the isolated bovine heart complex i
    • T. Ohnishi, J.E. Johnson, T. Yano, R. LoBrutto, and W.R. Widger Thermodynamic and EPR studies of slowly relaxing ubisemiquinone species in the isolated bovine heart complex I FEBS Lett. 579 2005 500 506
    • (2005) FEBS Lett. , vol.579 , pp. 500-506
    • Ohnishi, T.1    Johnson, J.E.2    Yano, T.3    LoBrutto, R.4    Widger, W.R.5
  • 90
    • 40549126917 scopus 로고    scopus 로고
    • Electrostatic interactions between FeS clusters in NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    • L. Euro, D.A. Bloch, M. Wikström, M.I. Verkhovsky, and M. Verkhovskaya Electrostatic interactions between FeS clusters in NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli Biochemistry 47 2008 3185 3193
    • (2008) Biochemistry , vol.47 , pp. 3185-3193
    • Euro, L.1    Bloch, D.A.2    Wikström, M.3    Verkhovsky, M.I.4    Verkhovskaya, M.5
  • 92
    • 0023645185 scopus 로고
    • EPR characterisation of the iron-sulfur clusters in the NADH:ubiquinone oxidoreductase segment of the respiratory chain in Paracoccus denitrificans
    • S.W. Meinhardt, T. Kula, T. Yagi, T. Lillich, and T. Ohnishi EPR characterisation of the iron-sulfur clusters in the NADH:ubiquinone oxidoreductase segment of the respiratory chain in Paracoccus denitrificans J. Biol. Chem. 262 1987 9147 9153
    • (1987) J. Biol. Chem. , vol.262 , pp. 9147-9153
    • Meinhardt, S.W.1    Kula, T.2    Yagi, T.3    Lillich, T.4    Ohnishi, T.5
  • 93
    • 0021099044 scopus 로고
    • Evidence of an ubisemiquinone radical(s) from the NADH-ubiquinone reductase of the mitochondrial respiratory chain
    • H. Suzuki, and T.E. King Evidence of an ubisemiquinone radical(s) from the NADH-ubiquinone reductase of the mitochondrial respiratory chain J. Biol. Chem. 258 1983 352 358
    • (1983) J. Biol. Chem. , vol.258 , pp. 352-358
    • Suzuki, H.1    King, T.E.2
  • 94
    • 0024435190 scopus 로고
    • Ubisemiquinone in the NADH-ubiquinone reductase region of the mitochondrial respiratory chain
    • D.S. Burbaev, I.A. Moroz, A.B. Kotlyar, V.D. Sled, and A.D. Vinogradov Ubisemiquinone in the NADH-ubiquinone reductase region of the mitochondrial respiratory chain FEBS Lett. 254 1989 47 51
    • (1989) FEBS Lett. , vol.254 , pp. 47-51
    • Burbaev, D.S.1    Moroz, I.A.2    Kotlyar, A.B.3    Sled, V.D.4    Vinogradov, A.D.5
  • 95
    • 0025349462 scopus 로고
    • Coupling site i and the rotenone-sensitive ubisemiquinone in tightly coupled submitochondrial particles
    • A.B. Kotlyar, V.D. Sled, D.S. Burbaev, I.A. Moroz, and A.D. Vinogradov Coupling site I and the rotenone-sensitive ubisemiquinone in tightly coupled submitochondrial particles FEBS Lett. 264 1990 17 20
    • (1990) FEBS Lett. , vol.264 , pp. 17-20
    • Kotlyar, A.B.1    Sled, V.D.2    Burbaev, D.S.3    Moroz, I.A.4    Vinogradov, A.D.5
  • 96
    • 0028214381 scopus 로고
    • Ubisemiquinones as obligatory intermediates in the electron transfer from NADH to ubiquinone
    • A.M.P. De Jong, and S.P.J. Albracht Ubisemiquinones as obligatory intermediates in the electron transfer from NADH to ubiquinone Eur. J. Biochem. 222 1994 975 982
    • (1994) Eur. J. Biochem. , vol.222 , pp. 975-982
    • De Jong, A.M.P.1    Albracht, S.P.J.2
  • 97
    • 0027994689 scopus 로고
    • Energy-induced structural changes in NADH:Q oxidoreductase of the mitochondrial respiratory chain
    • A.M.P. de Jong, A.B. Kotlyar, and S.P.J. Albracht Energy-induced structural changes in NADH:Q oxidoreductase of the mitochondrial respiratory chain Biochim. Biophys. Acta 1186 1994 163 171
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 163-171
    • De Jong, A.M.P.1    Kotlyar, A.B.2    Albracht, S.P.J.3
  • 98
    • 0031046751 scopus 로고    scopus 로고
    • The iron-sulfur clusters 2 and ubisemiquinone radicals of NADH:ubiquinone oxidoreductase are involved in energy coupling in submitochondrial particles
    • R. van Belzen, A.B. Kotlyar, N. Moon, W.R. Dunham, and S.P.J. Albracht The iron-sulfur clusters 2 and ubisemiquinone radicals of NADH:ubiquinone oxidoreductase are involved in energy coupling in submitochondrial particles Biochemistry 36 1997 886 893
    • (1997) Biochemistry , vol.36 , pp. 886-893
    • Van Belzen, R.1    Kotlyar, A.B.2    Moon, N.3    Dunham, W.R.4    Albracht, S.P.J.5
  • 99
    • 0034663582 scopus 로고    scopus 로고
    • Characterization of the complex i associated ubisemiquinone species: Toward the understanding of their functional roles in the electron/proton transfer reaction
    • T. Yano, S. Magnitsky, and T. Ohnishi Characterization of the complex I associated ubisemiquinone species: toward the understanding of their functional roles in the electron/proton transfer reaction Biochim. Biophys. Acta 1459 2000 299 304
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 299-304
    • Yano, T.1    Magnitsky, S.2    Ohnishi, T.3
  • 101
    • 77953811928 scopus 로고    scopus 로고
    • The role of a conserved tyrosine in the 49-kDa subunit of complex i for ubiquinone binding and reduction
    • M.A. Tocilescu, U. Fendel, K. Zwicker, S. Dröse, S. Kerscher, and U. Brandt The role of a conserved tyrosine in the 49-kDa subunit of complex I for ubiquinone binding and reduction Biochim. Biophys. Acta 1797 2010 625 632
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 625-632
    • Tocilescu, M.A.1    Fendel, U.2    Zwicker, K.3    Dröse, S.4    Kerscher, S.5    Brandt, U.6
  • 104
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • S. Stoll, and A. Schweiger EasySpin, a comprehensive software package for spectral simulation and analysis in EPR J. Magn. Reson. 178 2006 42 55
    • (2006) J. Magn. Reson. , vol.178 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2


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