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Volumn 42, Issue 4, 2010, Pages 261-278

The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited : I. Proposed consequences for electron transfer in the enzyme

Author keywords

Complex I; EPR; NADH:ubiquinone oxidoreductase; NADPH; Rapid kinetics

Indexed keywords

FLAVODOXIN; MITOCHONDRIAL PROTEIN; OXIDOREDUCTASE; PYRIDINE NUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UBIQUINONE;

EID: 77956059703     PISSN: 0145479X     EISSN: 15736881     Source Type: Journal    
DOI: 10.1007/s10863-010-9301-z     Document Type: Article
Times cited : (7)

References (117)
  • 1
    • 33751561773 scopus 로고    scopus 로고
    • Tight binding of NADPH to the 39-kDa subunit of complex i is not required for catalytic activity but stabilizes the multiprotein complex
    • A Abdrakhmanova K Zwicker S Kerscher V Zickermann U Brandt 2006 Tight binding of NADPH to the 39-kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex Biochim Biophys Acta 1757 1676 1682
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 1676-1682
    • Abdrakhmanova, A.1    Zwicker, K.2    Kerscher, S.3    Zickermann, V.4    Brandt, U.5
  • 2
    • 0016209718 scopus 로고
    • Some new paramagnetic centers in submitochondrial particles detectable by EPR spectroscopy
    • SPJ Albracht 1974 Some new paramagnetic centers in submitochondrial particles detectable by EPR spectroscopy Biochim Biophys Acta 347 183 192
    • (1974) Biochim Biophys Acta , vol.347 , pp. 183-192
    • Albracht, S.P.J.1
  • 3
    • 0019324015 scopus 로고
    • The prosthetic groups in succinate dehydrogenase. Number and stoichiometry
    • SPJ Albracht 1980 The prosthetic groups in succinate dehydrogenase. Number and stoichiometry Biochim Biophys Acta 612 11 28
    • (1980) Biochim Biophys Acta , vol.612 , pp. 11-28
    • Albracht, S.P.J.1
  • 6
    • 77956062836 scopus 로고    scopus 로고
    • The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited. II. Comparison of the proposed working hypothesis with literature data
    • doi: 10.1007/s10863-010-9302-y
    • Albracht SPJ (2010) The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited. II. Comparison of the proposed working hypothesis with literature data. J Bioener Biomem Accompanying paper. doi: 10.1007/s10863-010-9302-y
    • (2010) J Bioener Biomem Accompanying Paper.
    • Spj, A.1
  • 7
    • 0017729558 scopus 로고
    • The number of Fe atoms in the iron-sulphur centers of the respiratory chain
    • SPJ Albracht J Subramanian 1977 The number of Fe atoms in the iron-sulphur centers of the respiratory chain Biochim Biophys Acta 462 36 48
    • (1977) Biochim Biophys Acta , vol.462 , pp. 36-48
    • Albracht, S.P.J.1    Subramanian, J.2
  • 8
    • 0022518061 scopus 로고
    • Evidence for two independent pathways of electron transfer in mitochondrial NADH:Q oxidoreductase. II. Kinetics of reoxidation of the reduced enzyme
    • SPJ Albracht PT Bakker 1986 Evidence for two independent pathways of electron transfer in mitochondrial NADH:Q oxidoreductase. II. Kinetics of reoxidation of the reduced enzyme Biochim Biophys Acta 850 423 428
    • (1986) Biochim Biophys Acta , vol.850 , pp. 423-428
    • Albracht, S.P.J.1    Bakker, P.T.2
  • 9
    • 0031027369 scopus 로고    scopus 로고
    • Bovine-heart NADH:ubiquinone oxidoreductase is a monomer with 8 Fe-S clusters and 2 FMN groups
    • SPJ Albracht AMP De Jong 1997 Bovine-heart NADH:ubiquinone oxidoreductase is a monomer with 8 Fe-S clusters and 2 FMN groups Biochim Biophys Acta 1318 92 106
    • (1997) Biochim Biophys Acta , vol.1318 , pp. 92-106
    • Albracht, S.P.J.1    De Jong, A.M.P.2
  • 10
    • 0034680865 scopus 로고    scopus 로고
    • Learning from hydrogenases: Location of a proton pump and of a second FMN in bovine NADH-ubiquinone oxidoreductase (Complex I)
    • SPJ Albracht R Hedderich 2000 Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH-ubiquinone oxidoreductase (Complex I) FEBS Lett 485 1 6
    • (2000) FEBS Lett , vol.485 , pp. 1-6
    • Albracht, S.P.J.1    Hedderich, R.2
  • 12
    • 0018509972 scopus 로고
    • The stoichiometry of the iron-sulphur clusters 1a, 1b and 2 of NADH:Q oxidoreductase as present in beef-heart submitochondrial particles
    • SPJ Albracht FJ Leeuwerik B Van Swol 1979 The stoichiometry of the iron-sulphur clusters 1a, 1b and 2 of NADH:Q oxidoreductase as present in beef-heart submitochondrial particles FEBS Lett 104 197 200
    • (1979) FEBS Lett , vol.104 , pp. 197-200
    • Albracht, S.P.J.1    Leeuwerik, F.J.2    Van Swol, B.3
  • 13
    • 0019316133 scopus 로고
    • A comparison of the respiratory chain in particles from Paracoccus denitrificans and bovine heart mitochondria by EPR spectroscopy
    • SPJ Albracht HW Van Verseveld WR Hagen ML Kalkman 1980 A comparison of the respiratory chain in particles from Paracoccus denitrificans and bovine heart mitochondria by EPR spectroscopy Biochim Biophys Acta 593 173 186
    • (1980) Biochim Biophys Acta , vol.593 , pp. 173-186
    • Albracht, S.P.J.1    Van Verseveld, H.W.2    Hagen, W.R.3    Kalkman, M.L.4
  • 14
    • 0037422404 scopus 로고    scopus 로고
    • Quantitative amino acid analysis of bovine NADH:ubiquinone oxidoreductase (Complex I) and related enzymes. Consequences for the number of prosthetic groups
    • SPJ Albracht E Van der Linden BW Faber 2003 Quantitative amino acid analysis of bovine NADH:ubiquinone oxidoreductase (Complex I) and related enzymes. Consequences for the number of prosthetic groups Biochim Biophys Acta 1557 41 49
    • (2003) Biochim Biophys Acta , vol.1557 , pp. 41-49
    • Albracht, S.P.J.1    Van Der Linden, E.2    Faber, B.W.3
  • 15
    • 0022448493 scopus 로고
    • Evidence for two independent pathways of electron transfer in mitochondrial NADH:Q oxidoreductase. I. Pre-steady-state kinetics with NADPH
    • PT Bakker SPJ Albracht 1986 Evidence for two independent pathways of electron transfer in mitochondrial NADH:Q oxidoreductase. I. Pre-steady-state kinetics with NADPH Biochim Biophys Acta 850 413 422
    • (1986) Biochim Biophys Acta , vol.850 , pp. 413-422
    • Bakker, P.T.1    Albracht, S.P.J.2
  • 17
    • 0014184404 scopus 로고
    • The properties of dicyclohexylcarbodiimide as an inhibitor of oxidative phosphorylation
    • RB Beechey AM Roberton CT Holloway IG Knight 1967 The properties of dicyclohexylcarbodiimide as an inhibitor of oxidative phosphorylation Biochemistry 6 3867 3879
    • (1967) Biochemistry , vol.6 , pp. 3867-3879
    • Beechey, R.B.1    Roberton, A.M.2    Holloway, C.T.3    Knight, I.G.4
  • 18
    • 0020494651 scopus 로고
    • New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria
    • H Beinert SPJ Albracht 1982 New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria Biochim Biophys Acta 683 245 277
    • (1982) Biochim Biophys Acta , vol.683 , pp. 245-277
    • Beinert, H.1    Albracht, S.P.J.2
  • 19
    • 77956061551 scopus 로고
    • Kinetic studies on reduced diphosphopyridine nucleotide dehydrogenase by Electron Paramagnetic Resonance spectroscopy
    • H Beinert G Palmer T Cremona TP Singer 1965 Kinetic studies on reduced diphosphopyridine nucleotide dehydrogenase by Electron Paramagnetic Resonance spectroscopy J Biol Chem 240 475 480
    • (1965) J Biol Chem , vol.240 , pp. 475-480
    • Beinert, H.1    Palmer, G.2    Cremona, T.3    Singer, T.P.4
  • 20
    • 0028269382 scopus 로고
    • Catalytic sector of complex i (NADH:ubiquinone oxidoreductase): Subunit stoichiometry and substrate-induced conformation changes
    • G Belogrudov Y Hatefi 1994 Catalytic sector of complex I (NADH:ubiquinone oxidoreductase): subunit stoichiometry and substrate-induced conformation changes Biochemistry 33 4571 4576
    • (1994) Biochemistry , vol.33 , pp. 4571-4576
    • Belogrudov, G.1    Hatefi, Y.2
  • 21
    • 0029821089 scopus 로고    scopus 로고
    • Intersubunit interactions in the bovine mitochondrial complex i as revealed by ligand blotting
    • GI Belogrudov Y Hatefi 1996 Intersubunit interactions in the bovine mitochondrial complex I as revealed by ligand blotting Biochem Biophys Res Commun 227 135 139
    • (1996) Biochem Biophys Res Commun , vol.227 , pp. 135-139
    • Belogrudov, G.I.1    Hatefi, Y.2
  • 22
    • 70350351403 scopus 로고    scopus 로고
    • Structural basis for the mechanism of respiratory complex i
    • JM Berrisford LA Sazanov 2009 Structural basis for the mechanism of respiratory complex I J Biol Chem 284 29773 29783
    • (2009) J Biol Chem , vol.284 , pp. 29773-29783
    • Berrisford, J.M.1    Sazanov, L.A.2
  • 23
    • 0015505558 scopus 로고
    • Effect of N, N?-dicyclohexylcarbodiimide and other carbodiimides on electron transfer catalyzed by submitochondrial particles
    • RE Beyer TW Brink DL Crankshaw JM Kuner A Pasternak 1972 Effect of N, N?-dicyclohexylcarbodiimide and other carbodiimides on electron transfer catalyzed by submitochondrial particles Biochemistry 11 961 969
    • (1972) Biochemistry , vol.11 , pp. 961-969
    • Beyer, R.E.1    Brink, T.W.2    Crankshaw, D.L.3    Kuner, J.M.4    Pasternak, A.5
  • 24
    • 68749112864 scopus 로고    scopus 로고
    • The respiratory complexes i from the mitochondria of two Pichia species
    • HR Bridges L Grgic M Harbour J Hirst 2009 The respiratory complexes I from the mitochondria of two Pichia species Biochem J 422 151 159
    • (2009) Biochem J , vol.422 , pp. 151-159
    • Bridges, H.R.1    Grgic, L.2    Harbour, M.3    Hirst, J.4
  • 27
    • 0037422409 scopus 로고    scopus 로고
    • Two EPR-detectable [4Fe-4S] clusters, N2a and N2b, are bound to the NuoI (TYKY) subunit of NADH:ubiquinone oxidoreductase (Complex I) from Rhodobacter capsulatus
    • M Chevallet A Dupuis JP Issartel J Lunardi R Van Belzen SPJ Albracht 2003 Two EPR-detectable [4Fe-4S] clusters, N2a and N2b, are bound to the NuoI (TYKY) subunit of NADH:ubiquinone oxidoreductase (Complex I) from Rhodobacter capsulatus Biochim Biophys Acta 1557 51 66
    • (2003) Biochim Biophys Acta , vol.1557 , pp. 51-66
    • Chevallet, M.1    Dupuis, A.2    Issartel, J.P.3    Lunardi, J.4    Van Belzen, R.5    Albracht, S.P.J.6
  • 29
    • 0000854671 scopus 로고
    • Respiratory granules of heart muscle
    • KW Cleland EC Slater 1953 Respiratory granules of heart muscle Biochem J 53 547 556
    • (1953) Biochem J , vol.53 , pp. 547-556
    • Cleland, K.W.1    Slater, E.C.2
  • 30
    • 0000198662 scopus 로고
    • Studies on the respiratory chain-linked NADH dehydrogenase. VI. Further purification and properties of the enzyme from beef heart
    • T Cremona EB Kearney 1964 Studies on the respiratory chain-linked NADH dehydrogenase. VI. Further purification and properties of the enzyme from beef heart J Biol Chem 239 2328 2334
    • (1964) J Biol Chem , vol.239 , pp. 2328-2334
    • Cremona, T.1    Kearney, E.B.2
  • 31
    • 0032504107 scopus 로고    scopus 로고
    • The 49-kDa subunit of NADH-ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone-related inhibitors
    • E Darrouzet JP Issartel J Lunardi A Dupuis 1998 The 49-kDa subunit of NADH-ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone-related inhibitors FEBS Lett 431 34 38
    • (1998) FEBS Lett , vol.431 , pp. 34-38
    • Darrouzet, E.1    Issartel, J.P.2    Lunardi, J.3    Dupuis, A.4
  • 32
    • 0028214381 scopus 로고
    • Ubisemiquinones as obligatory intermediates in the electron transfer from NADH to ubiquinone
    • AMP De Jong SPJ Albracht 1994 Ubisemiquinones as obligatory intermediates in the electron transfer from NADH to ubiquinone Eur J Biochem 222 975 982
    • (1994) Eur J Biochem , vol.222 , pp. 975-982
    • De Jong, A.M.P.1    Albracht, S.P.J.2
  • 33
    • 0027994689 scopus 로고
    • Energy-induced structural changes in NADH:Q oxidoreductase of the mitochondrial respiratory chain
    • AMP De Jong AB Kotlyar SPJ Albracht 1994 Energy-induced structural changes in NADH:Q oxidoreductase of the mitochondrial respiratory chain Biochim Biophys Acta 1186 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
  • 34
    • 0034691658 scopus 로고    scopus 로고
    • Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica
    • R Djafarzadeh S Kerscher K Zwicker M Radermacher M Lindahl H Schägger U Brandt 2000 Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica Biochim Biophys Acta 1459 230 238
    • (2000) Biochim Biophys Acta , vol.1459 , pp. 230-238
    • Djafarzadeh, R.1    Kerscher, S.2    Zwicker, K.3    Radermacher, M.4    Lindahl, M.5    Schägger, H.6    Brandt, U.7
  • 35
    • 0016837080 scopus 로고
    • Oxidation of NADPH by submitochondrial particles from beef heart in complete absence of transhydrogenase activity from NADPH to NAD
    • L Djavadi-Ohaniance H Hatefi 1975 Oxidation of NADPH by submitochondrial particles from beef heart in complete absence of transhydrogenase activity from NADPH to NAD J Biol Chem 250 9397 9403
    • (1975) J Biol Chem , vol.250 , pp. 9397-9403
    • Djavadi-Ohaniance, L.1    Hatefi, H.2
  • 36
    • 0017198111 scopus 로고
    • Steady-state kinetics of high molecular weight (type-I) NADH dehydrogenase
    • G Dooijewaard EC Slater 1976 Steady-state kinetics of high molecular weight (type-I) NADH dehydrogenase Biochim Biophys Acta 440 1 15
    • (1976) Biochim Biophys Acta , vol.440 , pp. 1-15
    • Dooijewaard, G.1    Slater, E.C.2
  • 37
    • 0021665043 scopus 로고
    • Photoaffinity labelling of mitochondrial NADH dehydrogenase with arylazidoamorphigenin, an analogue of rotenone
    • FGP Earley CI Ragan 1984 Photoaffinity labelling of mitochondrial NADH dehydrogenase with arylazidoamorphigenin, an analogue of rotenone Biochem J 224 525 534
    • (1984) Biochem J , vol.224 , pp. 525-534
    • Earley, F.G.P.1    Ragan, C.I.2
  • 39
    • 0026484793 scopus 로고
    • Conservation of sequences of subunits of mitochondrial complex i and their relationships with other proteins
    • IM Fearnley JE Walker 1992 Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins Biochim Biophys Acta 1140 105 134
    • (1992) Biochim Biophys Acta , vol.1140 , pp. 105-134
    • Fearnley, I.M.1    Walker, J.E.2
  • 40
  • 41
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases
    • JC Fontecilla-Camps A Volbeda C Cavazza Y Nicolet 2007 Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases Chem Rev 107 4273 4303
    • (2007) Chem Rev , vol.107 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 42
    • 0034782745 scopus 로고    scopus 로고
    • Complex I: A chimaera of a redox and conformation-driven proton pump?
    • T Friedrich 2001 Complex I: a chimaera of a redox and conformation-driven proton pump? J Bioenerg Bioemembr 33 169 177
    • (2001) J Bioenerg Bioemembr , vol.33 , pp. 169-177
    • Friedrich, T.1
  • 43
    • 0018438631 scopus 로고
    • Purification and molecular and enzymic properties of mitochondrial NADH dehydrogenase
    • YM Galante Y Hatefi 1979 Purification and molecular and enzymic properties of mitochondrial NADH dehydrogenase Arch Biochem Biophys 192 559 568
    • (1979) Arch Biochem Biophys , vol.192 , pp. 559-568
    • Galante, Y.M.1    Hatefi, Y.2
  • 44
    • 0032588194 scopus 로고    scopus 로고
    • - stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles
    • - stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles FEBS Lett 451 157 161
    • (1999) FEBS Lett , vol.451 , pp. 157-161
    • Galkin, A.S.1    Grivennikova, V.G.2    Vinogradov, A.D.3
  • 45
    • 29744466425 scopus 로고
    • Deterermination of serum proteins by means of the biuret reaction
    • AG Gornall CJ Bardawill MM David 1949 Deterermination of serum proteins by means of the biuret reaction J Biol Chem 177 755 766
    • (1949) J Biol Chem , vol.177 , pp. 755-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 46
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22Å in ice
    • N Grigorieff 1998 Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22Å in ice J Mol Biol 277 1033 1046
    • (1998) J Mol Biol , vol.277 , pp. 1033-1046
    • Grigorieff, N.1
  • 47
    • 0031592480 scopus 로고    scopus 로고
    • Three-dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction
    • V Guénebaut R Vincentelli D Mills H Weiss KR Leonard 1997 Three-dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction J Mol Biol 265 409 418
    • (1997) J Mol Biol , vol.265 , pp. 409-418
    • Guénebaut, V.1    Vincentelli, R.2    Mills, D.3    Weiss, H.4    Leonard, K.R.5
  • 48
    • 0032512616 scopus 로고    scopus 로고
    • Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (Complex I)
    • V Guénebaut A Schlitt H Weiss K Leonard T Friedrich 1998 Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (Complex I) J Mol Biol 276 105 112
    • (1998) J Mol Biol , vol.276 , pp. 105-112
    • Guénebaut, V.1    Schlitt, A.2    Weiss, H.3    Leonard, K.4    Friedrich, T.5
  • 49
    • 0014961911 scopus 로고
    • Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. XVII. Reaction sites of piericidin A and rotenone
    • M Gutman TP Singer JE Casida 1970 Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. XVII. Reaction sites of piericidin A and rotenone J Biol Chem 245 1992 1997
    • (1970) J Biol Chem , vol.245 , pp. 1992-1997
    • Gutman, M.1    Singer, T.P.2    Casida, J.E.3
  • 50
    • 0014294151 scopus 로고
    • Flavoproteins of the electron transport system and the site of action of amytal, rotenone, and piericidin A
    • Y Hatefi 1968 Flavoproteins of the electron transport system and the site of action of amytal, rotenone, and piericidin A Proc Natl Acad Sci USA 60 733 740
    • (1968) Proc Natl Acad Sci USA , vol.60 , pp. 733-740
    • Hatefi, Y.1
  • 51
    • 0015930574 scopus 로고
    • Oxidation of reduced triphosphopyridine nucelotide by sbmitochondrial particles from beef heart
    • Y Hatefi 1973 Oxidation of reduced triphosphopyridine nucelotide by sbmitochondrial particles from beef heart Biochem Biophys Res Commun 50 978 984
    • (1973) Biochem Biophys Res Commun , vol.50 , pp. 978-984
    • Hatefi, Y.1
  • 52
    • 0017113595 scopus 로고
    • Electron paramagnetic resonance studies on the reduction of the components of complex i and transhydrogenase-inhibited complex i by NADH and NADPH
    • Y Hatefi AJ Bearden 1976 Electron paramagnetic resonance studies on the reduction of the components of complex I and transhydrogenase-inhibited complex I by NADH and NADPH Biochem Biophys Res Commun 69 1032 1038
    • (1976) Biochem Biophys Res Commun , vol.69 , pp. 1032-1038
    • Hatefi, Y.1    Bearden, A.J.2
  • 53
    • 0015864046 scopus 로고
    • Interactions of reduced and oxidized triphosphopyridine nucleotides with the electron-transport system of bovine heart mitochondria
    • Y Hatefi WG Hanstein 1973 Interactions of reduced and oxidized triphosphopyridine nucleotides with the electron-transport system of bovine heart mitochondria Biochemistry 12 3515 3522
    • (1973) Biochemistry , vol.12 , pp. 3515-3522
    • Hatefi, Y.1    Hanstein, W.G.2
  • 54
    • 0014195657 scopus 로고
    • Resolution of complex i (DPNH-coenzyme Q reductase) of the mitochondrial electron transfer system
    • Y Hatefi KE Stempel 1967 Resolution of complex I (DPNH-coenzyme Q reductase) of the mitochondrial electron transfer system Biochem Biophys Res Commun 26 301 308
    • (1967) Biochem Biophys Res Commun , vol.26 , pp. 301-308
    • Hatefi, Y.1    Stempel, K.E.2
  • 55
    • 0014669938 scopus 로고
    • Isolation and enzymatic properties of the mitochondrial reduced diphosphopyridine nucleotide dehydrogenase
    • Y Hatefi KE Stempel 1969 Isolation and enzymatic properties of the mitochondrial reduced diphosphopyridine nucleotide dehydrogenase J Biol Chem 244 2350 2357
    • (1969) J Biol Chem , vol.244 , pp. 2350-2357
    • Hatefi, Y.1    Stempel, K.E.2
  • 56
    • 0029988678 scopus 로고    scopus 로고
    • Nicotinamide nucleotide transhydrogenase: A model for utilization of substrate binding energy for proton translocation
    • Y Hatefi M Yamaguchi 1996 Nicotinamide nucleotide transhydrogenase: a model for utilization of substrate binding energy for proton translocation FASEB J 10 444 452
    • (1996) FASEB J , vol.10 , pp. 444-452
    • Hatefi, Y.1    Yamaguchi, M.2
  • 57
    • 0000948392 scopus 로고
    • Studies on the electron transfer system; XL. Preparation and properties of mitochondrial DPNH-Coenzyme Q reductase
    • Y Hatefi AG Haavik DE Griffiths 1962 Studies on the electron transfer system; XL. Preparation and properties of mitochondrial DPNH-Coenzyme Q reductase J Biol Chem 237 1667 1680
    • (1962) J Biol Chem , vol.237 , pp. 1667-1680
    • Hatefi, Y.1    Haavik, A.G.2    Griffiths, D.E.3
  • 58
    • 0019889304 scopus 로고
    • EPR spectral stimulation on cluster N-1b in NADH-ubiquinone oxidoreductase of bovine heart mitochondria
    • DO Hearshen WR Dunham SPJ Albracht T Ohnishi H Beinert 1981 EPR spectral stimulation on cluster N-1b in NADH-ubiquinone oxidoreductase of bovine heart mitochondria FEBS Lett 133 287 290
    • (1981) FEBS Lett , vol.133 , pp. 287-290
    • Hearshen, D.O.1    Dunham, W.R.2    Albracht, S.P.J.3    Ohnishi, T.4    Beinert, H.5
  • 59
    • 23044477952 scopus 로고    scopus 로고
    • Organization of iron-sulfur clusters in respiratory Complex i
    • P Hinchliffe LA Sazanov 2005 Organization of iron-sulfur clusters in respiratory Complex I Science 309 771 774
    • (2005) Science , vol.309 , pp. 771-774
    • Hinchliffe, P.1    Sazanov, L.A.2
  • 61
    • 0026077298 scopus 로고
    • Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I)
    • G Hofhaus H Weiss K Leonard 1991 Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I) J Mol Biol 221 1027 1043
    • (1991) J Mol Biol , vol.221 , pp. 1027-1043
    • Hofhaus, G.1    Weiss, H.2    Leonard, K.3
  • 62
    • 0025072729 scopus 로고
    • Slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase
    • AB Kotlyar AD Vinogradov 1990 Slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase Biochim Biophys Acta 1019 151 158
    • (1990) Biochim Biophys Acta , vol.1019 , pp. 151-158
    • Kotlyar, A.B.1    Vinogradov, A.D.2
  • 63
    • 0023030622 scopus 로고
    • Spectroscopic characterization of the number and type of iron-sulfur clusters in NADH:ubiquinone oxidoreductase
    • AT Kowal JE Morningstar MK Johnson RR Ramsay TP Singer 1986 Spectroscopic characterization of the number and type of iron-sulfur clusters in NADH:ubiquinone oxidoreductase J Biol Chem 261 9239 9245
    • (1986) J Biol Chem , vol.261 , pp. 9239-9245
    • Kowal, A.T.1    Morningstar, J.E.2    Johnson, M.K.3    Ramsay, R.R.4    Singer, T.P.5
  • 64
    • 0024297325 scopus 로고
    • Studies on the electron transfer pathway, topography of iron-sulfur centers, and site of coupling in NADH-Q oxidoreductase
    • G Krishnamoorthy PC Hinkle 1988 Studies on the electron transfer pathway, topography of iron-sulfur centers, and site of coupling in NADH-Q oxidoreductase J Biol Chem 263 17566 17575
    • (1988) J Biol Chem , vol.263 , pp. 17566-17575
    • Krishnamoorthy, G.1    Hinkle, P.C.2
  • 65
    • 0032490102 scopus 로고    scopus 로고
    • Quinone specificity of Complex i
    • G Lenaz 1998 Quinone specificity of Complex I Biochim Biophys Acta 1364 207 221
    • (1998) Biochim Biophys Acta , vol.1364 , pp. 207-221
    • Lenaz, G.1
  • 66
    • 0014410541 scopus 로고
    • Organice structural specificity and sites of Coenzyme Q in succinoxidase and DPNH-oxidase systems
    • G Lenaz GD Daves Jr K Folkers 1968 Organice structural specificity and sites of Coenzyme Q in succinoxidase and DPNH-oxidase systems Arch Biochem Biophys 123 539 550
    • (1968) Arch Biochem Biophys , vol.123 , pp. 539-550
    • Lenaz, G.1    Daves Jr., G.D.2    Folkers, K.3
  • 67
    • 0015013282 scopus 로고
    • Specificity of lipids and Coenzyme Q in mitochondrial NADH and succin-oxidase of beef heart and S. cerevisiae
    • G Lenaz A Castelli GP Littarru E Bertoli K Folkers 1971 Specificity of lipids and Coenzyme Q in mitochondrial NADH and succin-oxidase of beef heart and S. cerevisiae Arch Biochem Biophys 142 407 416
    • (1971) Arch Biochem Biophys , vol.142 , pp. 407-416
    • Lenaz, G.1    Castelli, A.2    Littarru, G.P.3    Bertoli, E.4    Folkers, K.5
  • 68
    • 0023136818 scopus 로고
    • Three-dimensional structure of NADH: Ubiquinone reductase (complex I) from Neurospora mitochondria determined by electron microscopy of membrane crystals
    • K Leonard H Haiker H Weiss 1987 Three-dimensional structure of NADH: ubiquinone reductase (complex I) from Neurospora mitochondria determined by electron microscopy of membrane crystals J Mol Biol 194 277 286
    • (1987) J Mol Biol , vol.194 , pp. 277-286
    • Leonard, K.1    Haiker, H.2    Weiss, H.3
  • 69
    • 50549169010 scopus 로고
    • Succinate-linked disphosphopyridine nucleotide reduction in submitochondrial particles
    • H Löw I Vallin 1963 Succinate-linked disphosphopyridine nucleotide reduction in submitochondrial particles Biochim Biophys Acta 69 361 374
    • (1963) Biochim Biophys Acta , vol.69 , pp. 361-374
    • Löw, H.1    Vallin, I.2
  • 70
    • 0001720216 scopus 로고
    • Studies on the respiratory chain-linked NADH dehydrogenase. VII; Labile sulfide groups in the dehydrogenase and in related proteins
    • CJ Lusty JM Machinist TP Singer 1965 Studies on the respiratory chain-linked NADH dehydrogenase. VII; Labile sulfide groups in the dehydrogenase and in related proteins J Biol Chem 240 1804 1810
    • (1965) J Biol Chem , vol.240 , pp. 1804-1810
    • Lusty, C.J.1    MacHinist, J.M.2    Singer, T.P.3
  • 71
    • 0000708694 scopus 로고
    • Hydrogen transfer between reduced diphosphopyridine nucleotide dehydrogenase and the respiratory chain. II. An initial lag in the oxidation of reduced diphosphopyridine nucleotide
    • S Minakami FJ Schindler RW Estabrook 1964 Hydrogen transfer between reduced diphosphopyridine nucleotide dehydrogenase and the respiratory chain. II. An initial lag in the oxidation of reduced diphosphopyridine nucleotide J Biol Chem 239 2049 2054
    • (1964) J Biol Chem , vol.239 , pp. 2049-2054
    • Minakami, S.1    Schindler, F.J.2    Estabrook, R.W.3
  • 72
    • 46349107838 scopus 로고    scopus 로고
    • Three-dimensional structure of respiratory complex i from Escherichia coli in ice in the presence of nucleotides
    • DJ Morgan LA Sazanov 2008 Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides Biochim Biophys Acta 1777 711 718
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 711-718
    • Morgan, D.J.1    Sazanov, L.A.2
  • 73
    • 34249684873 scopus 로고    scopus 로고
    • The ND1 subunit constructs the inhibitor binding domain in bovine heart mitochondrial complex i
    • M Murai A Ishihara T Nishioka T Yagi H Miyoshi 2007 The ND1 subunit constructs the inhibitor binding domain in bovine heart mitochondrial complex I Biochemistry 46 6409 6416
    • (2007) Biochemistry , vol.46 , pp. 6409-6416
    • Murai, M.1    Ishihara, A.2    Nishioka, T.3    Yagi, T.4    Miyoshi, H.5
  • 74
    • 0016687657 scopus 로고
    • Thermodynamic and EPR characterization of iron-sulfur centers in the NADH-ubiquinone segment of the mitochondrial respiratory chain in pigeon heart
    • T Ohnishi 1975 Thermodynamic and EPR characterization of iron-sulfur centers in the NADH-ubiquinone segment of the mitochondrial respiratory chain in pigeon heart Biochim Biophys Acta 387 475 490
    • (1975) Biochim Biophys Acta , vol.387 , pp. 475-490
    • Ohnishi, T.1
  • 76
    • 0032490089 scopus 로고    scopus 로고
    • Iron-sulfur clusters/semiquinones in Complex i
    • T Ohnishi 1998 Iron-sulfur clusters/semiquinones in Complex I Biochim Biophys Acta 1364 186 206
    • (1998) Biochim Biophys Acta , vol.1364 , pp. 186-206
    • Ohnishi, T.1
  • 77
    • 0019877322 scopus 로고
    • Iron-sulfur N-1 clusters studied in NADH-ubiquinone oxidoreductase and in soluble NADH dehydrogenase
    • T Ohnishi H Blum YM Galante Y Hatefi 1981 Iron-sulfur N-1 clusters studied in NADH-ubiquinone oxidoreductase and in soluble NADH dehydrogenase J Biol Chem 256 9216 9220
    • (1981) J Biol Chem , vol.256 , pp. 9216-9220
    • Ohnishi, T.1    Blum, H.2    Galante, Y.M.3    Hatefi, Y.4
  • 78
    • 0015229035 scopus 로고
    • EPR detectable electron acceptors in submitochondrial particles from beef heart with specific reference to the iron-sulfur components of DPNH-ubiquinone reductase
    • NR Orme-Johnson WH Orme-Johnson RE Hansen H Beinert Y Hatefi 1971 EPR detectable electron acceptors in submitochondrial particles from beef heart with specific reference to the iron-sulfur components of DPNH-ubiquinone reductase Biochem Biophys Res Commun 44 446 452
    • (1971) Biochem Biophys Res Commun , vol.44 , pp. 446-452
    • Orme-Johnson, N.R.1    Orme-Johnson, W.H.2    Hansen, R.E.3    Beinert, H.4    Hatefi, Y.5
  • 79
    • 0016379120 scopus 로고
    • Electron paramagnetic resonance-detectable electron acceptors in beef heart mitochondria. Reduced diphosphopyridine nucleotide ubiquinone reductase segment of the electron transfer system
    • NR Orme-Johnson RE Hansen H Beinert 1974 Electron paramagnetic resonance-detectable electron acceptors in beef heart mitochondria. Reduced diphosphopyridine nucleotide ubiquinone reductase segment of the electron transfer system J Biol Chem 249 1922 1927
    • (1974) J Biol Chem , vol.249 , pp. 1922-1927
    • Orme-Johnson, N.R.1    Hansen, R.E.2    Beinert, H.3
  • 80
    • 0016379513 scopus 로고
    • Electron paramagnetic resonance-detectable electron acceptors in beef heart mitochondria. Ubihydroquinone-cytochrome c reductase segment of the electron transfer system and complex mitochondrial fragments
    • NR Orme-Johnson RE Hansen H Beinert 1974 Electron paramagnetic resonance-detectable electron acceptors in beef heart mitochondria. Ubihydroquinone-cytochrome c reductase segment of the electron transfer system and complex mitochondrial fragments J Biol Chem 249 1928 1939
    • (1974) J Biol Chem , vol.249 , pp. 1928-1939
    • Orme-Johnson, N.R.1    Hansen, R.E.2    Beinert, H.3
  • 81
    • 0019876754 scopus 로고
    • Structural identification of the iron-sulfur clusters of the respiratory chain-linked NADH dehydrogenase
    • C Paech JR Reynolds TP Singer RH Holm 1981 Structural identification of the iron-sulfur clusters of the respiratory chain-linked NADH dehydrogenase J Biol Chem 256 3167 3170
    • (1981) J Biol Chem , vol.256 , pp. 3167-3170
    • Paech, C.1    Reynolds, J.R.2    Singer, T.P.3    Holm, R.H.4
  • 83
    • 0037452914 scopus 로고    scopus 로고
    • Isolation, characterization and electron microscopic single particle analysis of the NADH:ubiquinone oxidoreductase (complex I) from the hyperthermophilic eubacterium Aquifex aeolicus
    • G Peng G Fritzsch V Zickermann H Schagger R Mentele F Lottspeich M Bostina M Radermacher R Huber KO Stetter H Michel 2003 Isolation, characterization and electron microscopic single particle analysis of the NADH:ubiquinone oxidoreductase (complex I) from the hyperthermophilic eubacterium Aquifex aeolicus Biochemistry 42 3032 3039
    • (2003) Biochemistry , vol.42 , pp. 3032-3039
    • Peng, G.1    Fritzsch, G.2    Zickermann, V.3    Schagger, H.4    Mentele, R.5    Lottspeich, F.6    Bostina, M.7    Radermacher, M.8    Huber, R.9    Stetter, K.O.10    Michel, H.11
  • 84
    • 0026032458 scopus 로고
    • Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase
    • SJ Pilkington JM Skehel RB Gennis JE Walker 1991 Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase Biochemistry 30 2166 2175
    • (1991) Biochemistry , vol.30 , pp. 2166-2175
    • Pilkington, S.J.1    Skehel, J.M.2    Gennis, R.B.3    Walker, J.E.4
  • 85
    • 0035795163 scopus 로고    scopus 로고
    • Evidence for a quinone binding site close to the interface between NUOD and NUOB subunits of Complex i
    • I Prieur J Lunardi A Dupuis 2001 Evidence for a quinone binding site close to the interface between NUOD and NUOB subunits of Complex I Biochim Biophys Acta 1504 173 178
    • (2001) Biochim Biophys Acta , vol.1504 , pp. 173-178
    • Prieur, I.1    Lunardi, J.2    Dupuis, A.3
  • 86
    • 33646678212 scopus 로고    scopus 로고
    • The three-dimensional structure of complex i from Yarrowia lipolytica: A highly dynamic enzyme
    • M Radermacher T Ruiz T Clason S Benjamin U Brandt V Zickermann 2006 The three-dimensional structure of complex I from Yarrowia lipolytica: a highly dynamic enzyme J Struct Biol 154 269 279
    • (2006) J Struct Biol , vol.154 , pp. 269-279
    • Radermacher, M.1    Ruiz, T.2    Clason, T.3    Benjamin, S.4    Brandt, U.5    Zickermann, V.6
  • 87
    • 0017169607 scopus 로고
    • The interaction of reduced nicotinamide-adenine dinucleotide phosphate with reduced nicotinamide-adenine dinucleotide-ubiquinone reductase from bovine heart mitochondria
    • CI Ragan 1976 The interaction of reduced nicotinamide-adenine dinucleotide phosphate with reduced nicotinamide-adenine dinucleotide-ubiquinone reductase from bovine heart mitochondria Biochem J 158 149 151
    • (1976) Biochem J , vol.158 , pp. 149-151
    • Ragan, C.I.1
  • 88
    • 0016231902 scopus 로고
    • Pyridine nucleotide transhydrogenase activity of soluble cardiac NADH dehydrogenase and particulate NADH-ubiquinone reductase
    • CI Ragan WR Widger TE King 1974 Pyridine nucleotide transhydrogenase activity of soluble cardiac NADH dehydrogenase and particulate NADH-ubiquinone reductase Biochem Biophys Res Commun 60 894 900
    • (1974) Biochem Biophys Res Commun , vol.60 , pp. 894-900
    • Ragan, C.I.1    Widger, W.R.2    King, T.E.3
  • 90
    • 50549155572 scopus 로고
    • Isolation and properties of the DPNH dehydrogenase of the respiratory chain from heart mitochondria
    • RL Ringler S Minakami TP Singer 1960 Isolation and properties of the DPNH dehydrogenase of the respiratory chain from heart mitochondria Biochem Biophys Res Commun 3 417 422
    • (1960) Biochem Biophys Res Commun , vol.3 , pp. 417-422
    • Ringler, R.L.1    Minakami, S.2    Singer, T.P.3
  • 91
    • 73649192336 scopus 로고
    • Studies on the respiratory chain-linked NADH dehydrogenase. II. Isolation and molecular properties of the enzyme from beef heart
    • RL Ringler S Minakami TP Singer 1963 Studies on the respiratory chain-linked NADH dehydrogenase. II. Isolation and molecular properties of the enzyme from beef heart J Biol Chem 238 801 810
    • (1963) J Biol Chem , vol.238 , pp. 801-810
    • Ringler, R.L.1    Minakami, S.2    Singer, T.P.3
  • 92
    • 0015220130 scopus 로고
    • Steady-state kinetics of mitochondrial nicotinamide nucleotide transhydrogenase. 2. The energy-linked reaction
    • J Rydström A Teixeira da Cruz L Ernster 1971 Steady-state kinetics of mitochondrial nicotinamide nucleotide transhydrogenase. 2. The energy-linked reaction Eur J Biochem 23 213 219
    • (1971) Eur J Biochem , vol.23 , pp. 213-219
    • Rydström, J.1    Teixeira Da Cruz, A.2    Ernster, L.3
  • 93
    • 0017838907 scopus 로고
    • The mechanism of oxidation of reduced nicotinamide dinucleotide phosphate by submitochondrial particles from beef heart
    • J Rydström J Montelius D Bäckström L Ernster 1978 The mechanism of oxidation of reduced nicotinamide dinucleotide phosphate by submitochondrial particles from beef heart Biochim Biophys Acta 501 370 380
    • (1978) Biochim Biophys Acta , vol.501 , pp. 370-380
    • Rydström, J.1    Montelius, J.2    Bäckström, D.3    Ernster, L.4
  • 94
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory Complex i from Thermus thermophilus
    • LA Sazanov P Hinchliffe 2006 Structure of the hydrophilic domain of respiratory Complex I from Thermus thermophilus Science 311 1430 1436
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 95
    • 0033600871 scopus 로고    scopus 로고
    • A reductase/isomerase subunit of mitochondrial NADH:ubiquinone oxidoreductase (complex I) carries an NADPH and is involved in the biogenesis of the complex
    • U Schulte V Haupt A Abelmann W Fecke B Brors T Rasmussen T Friedrich H Weiss 1999 A reductase/isomerase subunit of mitochondrial NADH:ubiquinone oxidoreductase (complex I) carries an NADPH and is involved in the biogenesis of the complex J Mol Biol 292 569 580
    • (1999) J Mol Biol , vol.292 , pp. 569-580
    • Schulte, U.1    Haupt, V.2    Abelmann, A.3    Fecke, W.4    Brors, B.5    Rasmussen, T.6    Friedrich, T.7    Weiss, H.8
  • 96
    • 0018400873 scopus 로고
    • Mitochondrial electron-transport inhibitors
    • TP Singer 1979 Mitochondrial electron-transport inhibitors Meth Enzymol 55 454 462
    • (1979) Meth Enzymol , vol.55 , pp. 454-462
    • Singer, T.P.1
  • 98
    • 0024981157 scopus 로고
    • The pathway of electron transfer in NADH:Q oxidoreductase
    • R Van Belzen SPJ Albracht 1989 The pathway of electron transfer in NADH:Q oxidoreductase Biochim Biophys Acta 974 311 320
    • (1989) Biochim Biophys Acta , vol.974 , pp. 311-320
    • Van Belzen, R.1    Albracht, S.P.J.2
  • 99
    • 0025311855 scopus 로고
    • New evidence for the dimeric nature of NADH:Q oxidoreductase in bovine-heart submitochondrial particles
    • R Van Belzen MC Van Gaalen PA Cuypers SPJ Albracht 1990 New evidence for the dimeric nature of NADH:Q oxidoreductase in bovine-heart submitochondrial particles Biochim Biophys Acta 1017 152 159
    • (1990) Biochim Biophys Acta , vol.1017 , pp. 152-159
    • Van Belzen, R.1    Van Gaalen, M.C.2    Cuypers, P.A.3    Albracht, S.P.J.4
  • 100
    • 0026495482 scopus 로고
    • On the stoichiometry of the iron-sulphur clusters in mitochondrial NADH:ubiquinone oxidoreductase
    • R Van Belzen AMP De Jong SPJ Albracht 1992 On the stoichiometry of the iron-sulphur clusters in mitochondrial NADH:ubiquinone oxidoreductase Eur J Biochem 209 1019 1022
    • (1992) Eur J Biochem , vol.209 , pp. 1019-1022
    • Van Belzen, R.1    De Jong, A.M.P.2    Albracht, S.P.J.3
  • 101
    • 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 AB Kotlyar N Moon WR Dunham SPJ Albracht 1997 The iron-sulfur clusters 2 and ubisemiquinone radicals of NADH:ubiquinone oxidoreductase are involved in energy coupling in submitochondrial particles Biochemistry 36 886 893
    • (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
  • 103
    • 0014011854 scopus 로고
    • Molecular proportion of the fixed cytochrome components of the respiratory chain of Keilin-Hartree particles and beef heart mitochondria
    • WH Vanneste 1966 Molecular proportion of the fixed cytochrome components of the respiratory chain of Keilin-Hartree particles and beef heart mitochondria Biochim Biophys Acta 113 175 178
    • (1966) Biochim Biophys Acta , vol.113 , pp. 175-178
    • Vanneste, W.H.1
  • 106
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • JE Walker 1992 The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains Q Rev Biophys 25 253 324
    • (1992) Q Rev Biophys , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 107
    • 0026487290 scopus 로고
    • Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction
    • JE Walker JM Arizmendi A Dupuis IM Fearnley M Finel SM Medd SJ Pilkington MJ Runswick JM Skehel 1992 Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction J Mol Biol 226 1051 1072
    • (1992) J Mol Biol , vol.226 , pp. 1051-1072
    • Walker, J.E.1    Arizmendi, J.M.2    Dupuis, A.3    Fearnley, I.M.4    Finel, M.5    Medd, S.M.6    Pilkington, S.J.7    Runswick, M.J.8    Skehel, J.M.9
  • 108
    • 0021769852 scopus 로고
    • Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone
    • M Wikström 1984 Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone FEBS Lett 169 300 304
    • (1984) FEBS Lett , vol.169 , pp. 300-304
    • Wikström, M.1
  • 109
    • 0023274011 scopus 로고
    • Inhibition of NADH-ubiquinone reductase activity by N, N?-dicyclohexylcarbodiimide and correlation of this inhibition with the occurrence of energy-coupling site 1 in various organisms
    • T Yagi 1987 Inhibition of NADH-ubiquinone reductase activity by N, N?- dicyclohexylcarbodiimide and correlation of this inhibition with the occurrence of energy-coupling site 1 in various organisms Biochemistry 26 2822 2828
    • (1987) Biochemistry , vol.26 , pp. 2822-2828
    • Yagi, T.1
  • 110
    • 0023724205 scopus 로고
    • Identification of the dicyclohexylcarbodiimide-binding subunit of NADH- ubiquinone oxidoreductase (Complex I)
    • T Yagi Y Hatefi 1988 Identification of the dicyclohexylcarbodiimide- binding subunit of NADH- ubiquinone oxidoreductase (Complex I) J Biol Chem 263 16150 16155
    • (1988) J Biol Chem , vol.263 , pp. 16150-16155
    • Yagi, T.1    Hatefi, Y.2
  • 111
    • 0037418550 scopus 로고    scopus 로고
    • The Proton-Translocating NADH-Quinone Oxidoreductase in the Respiratory Chain: The Secret Unlocked
    • T Yagi A Matsuno-Yagi 2003 The Proton-Translocating NADH-Quinone Oxidoreductase in the Respiratory Chain: The Secret Unlocked Biochemistry 42 2266 2274
    • (2003) Biochemistry , vol.42 , pp. 2266-2274
    • Yagi, T.1    Matsuno-Yagi, A.2
  • 112
    • 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 J Hirst 2007 Reevaluating the relationship between EPR spectra and enzyme structure for the iron-sulfur clusters in NADH:quinone oxidoreductase Proc Natl Acad Sci USA 104 1270 12725
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1270-12725
    • Yakovlev, G.1    Reda, T.2    Hirst, J.3
  • 113
    • 0032478597 scopus 로고    scopus 로고
    • Mitochondrial NADH-ubiquinone oxidoreductase (Complex I). Effect of substrates on the fragmentation of subunits by trypsin
    • M Yamaguchi GI Belogrudov Y Hatefi 1998 Mitochondrial NADH-ubiquinone oxidoreductase (Complex I). Effect of substrates on the fragmentation of subunits by trypsin J Biol Chem 273 8094 8098
    • (1998) J Biol Chem , vol.273 , pp. 8094-8098
    • Yamaguchi, M.1    Belogrudov, G.I.2    Hatefi, Y.3
  • 114
    • 0033979304 scopus 로고    scopus 로고
    • The multiple nicotinamide nucleotide-binding subunits of bovine heart mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • M Yamaguchi GI Belogrudov A Matsuno-Yagi Y Hatefi 2000 The multiple nicotinamide nucleotide-binding subunits of bovine heart mitochondrial NADH:ubiquinone oxidoreductase (complex I) Eur J Biochem 267 329 336
    • (2000) Eur J Biochem , vol.267 , pp. 329-336
    • Yamaguchi, M.1    Belogrudov, G.I.2    Matsuno-Yagi, A.3    Hatefi, Y.4
  • 115
    • 0037844859 scopus 로고    scopus 로고
    • Characterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in the Nqo3 subunit of the proton-translocating NADH-ubiquinone oxidoreductase from Paracoccus denitrificans
    • T Yano J Sklar E Nakamaru-Ogiso Y Takahashi T Yagi T Ohnishi 2003 Characterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in the Nqo3 subunit of the proton-translocating NADH-ubiquinone oxidoreductase from Paracoccus denitrificans J Biol Chem 278 15514 15522
    • (2003) J Biol Chem , vol.278 , pp. 15514-15522
    • Yano, T.1    Sklar, J.2    Nakamaru-Ogiso, E.3    Takahashi, Y.4    Yagi, T.5    Ohnishi, T.6
  • 116
    • 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 1744 1754
    • (2005) Biochemistry , vol.44 , pp. 1744-1754
    • Yano, T.1    Dunham, W.H.2    Ohnishi, T.3


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