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Volumn 9, Issue 4, 1999, Pages 476-484

Structure of the respiratory NADH:ubiquinone oxidoreductase (complex I)

Author keywords

[No Author keywords available]

Indexed keywords

REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UBIQUINONE;

EID: 0033179604     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)80067-0     Document Type: Article
Times cited : (92)

References (115)
  • 1
    • 0000967140 scopus 로고
    • Flavin mononucleotide: The coenzyme of reduced diphosphopyridine nucleotide dehydrogenase
    • Rao NA, Felton SP, Huennekens FM, Mackler B: Flavin mononucleotide: The coenzyme of reduced diphosphopyridine nucleotide dehydrogenase. J Biol Chem 1963, 238:449-455.
    • (1963) J Biol Chem , vol.238 , pp. 449-455
    • Rao, N.A.1    Felton, S.P.2    Huennekens, F.M.3    Mackler, B.4
  • 2
    • 0002727146 scopus 로고
    • Mitochondrial iron-sulfur flavodehydrogenases
    • Edited by Capaldi RA. New York: Marcel Dekker
    • Ohnishi T: Mitochondrial iron-sulfur flavodehydrogenases. In Membrane Proteins in Energy Transduction. Edited by Capaldi RA. New York: Marcel Dekker; 1979:1-87.
    • (1979) Membrane Proteins in Energy Transduction , pp. 1-87
    • Ohnishi, T.1
  • 3
    • 0000283680 scopus 로고
    • Iron-sulfur clusters in the mitochondrial electron-transport chain
    • Edited by Spiro TG. New York: John Wiley & Sons
    • Ohnishi T, Salerno JC: Iron-sulfur clusters in the mitochondrial electron-transport chain. In Iron-Sulfur Proteins. Edited by Spiro TG. New York: John Wiley & Sons; 1982:285-327.
    • (1982) Iron-Sulfur Proteins , pp. 285-327
    • Ohnishi, T.1    Salerno, J.C.2
  • 4
    • 0020494651 scopus 로고
    • New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria
    • Beinert H, Albracht SPJ: New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria. Biochim Biophys Acta 1982, 683:245-277.
    • (1982) Biochim Biophys Acta , vol.683 , pp. 245-277
    • Beinert, H.1    Albracht, S.P.J.2
  • 5
    • 0032490089 scopus 로고    scopus 로고
    • Iron-sulfur clusters/semiquinones in complex I
    • A topical and recent review on electron paramagnetic resonance (EPR)-detectable iron-sulfur clusters and ubiquinones in bacterial and eukaryotic complex I
    • Ohnishi T: Iron-sulfur clusters/semiquinones in complex I. Biochim Biophys Acta 1998, 1364:186-206. A topical and recent review on electron paramagnetic resonance (EPR)-detectable iron-sulfur clusters and ubiquinones in bacterial and eukaryotic complex I.
    • (1998) Biochim Biophys Acta , vol.1364 , pp. 186-206
    • Ohnishi, T.1
  • 6
    • 0021099044 scopus 로고
    • Evidence of an ubisemiquinone radical(s) from the NADH-ubiquinone reductase of the mitochondrial respiratory chain
    • Suzuki H, King TE: Evidence of an ubisemiquinone radical(s) from the NADH-ubiquinone reductase of the mitochondrial respiratory chain. J Biol Chem 1983, 258:352-358.
    • (1983) J Biol Chem , vol.258 , pp. 352-358
    • Suzuki, H.1    King, T.E.2
  • 7
    • 0024435190 scopus 로고
    • Ubisemiquinone in the NADH-ubiquinone reductase region of the mitochondrial respiratory chain
    • Burbaev DS, Moroz IA, Kotlyar AB, Sled VD, Vinogradov AD: Ubisemiquinone in the NADH-ubiquinone reductase region of the mitochondrial respiratory chain. FEBS Lett 1989, 254:47-51.
    • (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
  • 8
    • 0028214381 scopus 로고
    • Ubisemiquinones as obligatory intermediates in the electron transfer from NADH to ubiquinone
    • De Jong AMP, Albracht SPJ: Ubisemiquinones as obligatory intermediates in the electron transfer from NADH to ubiquinone. Eur J Biochem 1994, 222:975-982.
    • (1994) Eur J Biochem , vol.222 , pp. 975-982
    • De Jong, A.M.P.1    Albracht, S.P.J.2
  • 9
    • 0017406329 scopus 로고
    • Control of the reverse electron transfer in submitochondrial particles by free energy
    • Rottenberg H, Gutman M: Control of the reverse electron transfer in submitochondrial particles by free energy. Biochemistry 1977, 16:3220-3227.
    • (1977) Biochemistry , vol.16 , pp. 3220-3227
    • Rottenberg, H.1    Gutman, M.2
  • 10
    • 0018119866 scopus 로고
    • 2+ uptake coupled to electron transport in rat heart mitochondria
    • 2+ uptake coupled to electron transport in rat heart mitochondria. J Biol Chem 1978, 253:6379-6385.
    • (1978) J Biol Chem , vol.253 , pp. 6379-6385
    • Vercesi, A.1    Reynafarje, B.2    Lehninger, A.L.3
  • 12
    • 0020490541 scopus 로고
    • + pump by exogenous quinones in intact mitochondria
    • + pump by exogenous quinones in intact mitochondria. J Biol Chem 1982, 257:4106-4113.
    • (1982) J Biol Chem , vol.257 , pp. 4106-4113
    • Di Virgilio, F.1    Azzone, G.F.2
  • 13
    • 0021754261 scopus 로고
    • Energetics of ATP-driven reverse electron-transfer from cytochrome c to fumarate and from succinate to NAD in submitochondrial particles
    • Scholes TA, Hinkle PC: Energetics of ATP-driven reverse electron-transfer from cytochrome c to fumarate and from succinate to NAD in submitochondrial particles. Biochemistry 1984, 23:3341-3345.
    • (1984) Biochemistry , vol.23 , pp. 3341-3345
    • Scholes, T.A.1    Hinkle, P.C.2
  • 14
    • 0021769852 scopus 로고
    • Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone
    • Wikström M: Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone. FEBS Lett 1984, 169:300-304.
    • (1984) FEBS Lett , vol.169 , pp. 300-304
    • Wikström, M.1
  • 15
    • 0023644782 scopus 로고
    • Upper and lower limits of the charge translocation stoichiometry of mitochondrial electron transport
    • Beavis AD: Upper and lower limits of the charge translocation stoichiometry of mitochondrial electron transport. J Biol Chem 1987, 262:6165-6173.
    • (1987) J Biol Chem , vol.262 , pp. 6165-6173
    • Beavis, A.D.1
  • 16
    • 0024023239 scopus 로고
    • Proton-electron stoichiometry of mitochondrial complex I estimated from the equilibrium thermodynamic force ratio
    • Brown GC, Brand MD: Proton-electron stoichiometry of mitochondrial complex I estimated from the equilibrium thermodynamic force ratio. Biochem J 1988, 252:473-479.
    • (1988) Biochem J , vol.252 , pp. 473-479
    • Brown, G.C.1    Brand, M.D.2
  • 17
    • 0025991887 scopus 로고
    • Redox-linked proton translocation by NADH-ubiquinone reductase (complex I)
    • Weiss H, Friedrich T: Redox-linked proton translocation by NADH-ubiquinone reductase (complex I). J Bioenerg Biomembr 1991, 23:743-754.
    • (1991) J Bioenerg Biomembr , vol.23 , pp. 743-754
    • Weiss, H.1    Friedrich, T.2
  • 18
    • 0027104114 scopus 로고
    • The NADH-ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker JE: The NADH-ubiquinone oxidoreductase (complex I) of respiratory chains. Q Rev Biophys 1992, 25:253-324.
    • (1992) Q Rev Biophys , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 20
    • 0032490105 scopus 로고    scopus 로고
    • Complex I from the fungus Neurospora crassa
    • Videira A: Complex I from the fungus Neurospora crassa. Biochim Biophys Acta 1998, 1364:89-100.
    • (1998) Biochim Biophys Acta , vol.1364 , pp. 89-100
    • Videira, A.1
  • 23
    • 0031765679 scopus 로고    scopus 로고
    • NADH:ubiquinone oxidoreductase from bovine heart mitochondria: Sequence of a novel 17.2-kDa subunit
    • Skehel JM, Fearnley IM, Walker JE: NADH:ubiquinone oxidoreductase from bovine heart mitochondria: Sequence of a novel 17.2-kDa subunit. FEBS Lett 1998, 438:301-305.
    • (1998) FEBS Lett , vol.438 , pp. 301-305
    • Skehel, J.M.1    Fearnley, I.M.2    Walker, J.E.3
  • 24
    • 0029075136 scopus 로고
    • Isolation and characterization of the proton-translocating NADH-ubiquinone oxidoreductase from Escherichia coli
    • Leif H, Sled VD, Ohnishi T, Weiss H, Friedrich T: Isolation and characterization of the proton-translocating NADH-ubiquinone oxidoreductase from Escherichia coli. Eur J Biochem 1995, 230:538-548.
    • (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
  • 25
    • 0023136818 scopus 로고
    • Three-dimensional structure of NADH: Ubiquinone reductase (complex I) from Neurospora mitochondria determined by electron microscopy of membrane crystals
    • Leonard K, Haiker H, Weiss H: Three-dimensional structure of NADH: ubiquinone reductase (complex I) from Neurospora mitochondria determined by electron microscopy of membrane crystals. J Mol Biol 1987, 194:277-286.
    • (1987) J Mol Biol , vol.194 , pp. 277-286
    • Leonard, K.1    Haiker, H.2    Weiss, H.3
  • 26
    • 0025760073 scopus 로고
    • The respiratory chain NADH dehydrogenase (complex I) of mitochondria
    • Weiss H, Friedrich T, Hofhaus G, Preis D: The respiratory chain NADH dehydrogenase (complex I) of mitochondria. Eur J Biochem 1991, 197:563-576.
    • (1991) Eur J Biochem , vol.197 , pp. 563-576
    • Weiss, H.1    Friedrich, T.2    Hofhaus, G.3    Preis, D.4
  • 27
    • 0027519561 scopus 로고
    • The gene locus of the proton-translocating NADH-ubiquinone oxidoreductase in Escherichia coli - Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I
    • Weidner U, Geier S, Ptock A, Friedrich T, Leif H, Weiss H: The gene locus of the proton-translocating NADH-ubiquinone oxidoreductase in Escherichia coli - Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I. J Mol Biol 1993, 233:109-122.
    • (1993) J Mol Biol , vol.233 , pp. 109-122
    • Weidner, U.1    Geier, S.2    Ptock, A.3    Friedrich, T.4    Leif, H.5    Weiss, H.6
  • 29
    • 0032539640 scopus 로고    scopus 로고
    • Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    • Braun M, Bungert S, Friedrich T: Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochemistry 1998, 37:1861-1867.
    • (1998) Biochemistry , vol.37 , pp. 1861-1867
    • Braun, M.1    Bungert, S.2    Friedrich, T.3
  • 30
    • 0030859256 scopus 로고    scopus 로고
    • Buchnera aphidicola (endosymbiont of aphids) contains nuoC(D) genes that encode subunits of NADH dehydrogenase
    • Clark MA, Baumann L, Baumann P: Buchnera aphidicola (endosymbiont of aphids) contains nuoC(D) genes that encode subunits of NADH dehydrogenase. Curr Microbiol 1997, 35:122-123.
    • (1997) Curr Microbiol , vol.35 , pp. 122-123
    • Clark, M.A.1    Baumann, L.2    Baumann, P.3
  • 31
    • 0027268344 scopus 로고
    • Characteristics of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans as revealed by biochemical, biophysical, and molecular biological approaches
    • Yagi T, Yano T, Matsuno-Yagi A: Characteristics of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans as revealed by biochemical, biophysical, and molecular biological approaches. J Bioenerg Biomembr 1993, 25:339-345.
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 339-345
    • Yagi, T.1    Yano, T.2    Matsuno-Yagi, A.3
  • 32
    • 0031041453 scopus 로고    scopus 로고
    • The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8 - Complete DNA sequence of the gene cluster and thermostable properties of the expressed NQ02 subunit
    • Yano T, Chu SS, Sled VD, Ohnishi T, Yagi T: The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8 - Complete DNA sequence of the gene cluster and thermostable properties of the expressed NQ02 subunit. J Biol Chem 1997, 272:4201-4211.
    • (1997) J Biol Chem , vol.272 , pp. 4201-4211
    • Yano, T.1    Chu, S.S.2    Sled, V.D.3    Ohnishi, T.4    Yagi, T.5
  • 34
    • 0029059910 scopus 로고
    • The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts
    • Friedrich T, Steinmüller K, Weiss H: The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts. FEBS Lett 1995, 367:107-111.
    • (1995) FEBS Lett , vol.367 , pp. 107-111
    • Friedrich, T.1    Steinmüller, K.2    Weiss, H.3
  • 38
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S, Ostermeier C, Ludwig B, Michel H: Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 1995, 376:660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 39
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 Angstrom resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment
    • Ostermeier C, Harrenga A, Ermler U, Michel H: Structure at 2.7 Angstrom resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment. Proc Natl Acad Sci USA 1997, 94:10547-10553.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2    Ermler, U.3    Michel, H.4
  • 43
    • 0031592480 scopus 로고    scopus 로고
    • Three dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction
    • The authors present the first three-dimensional structure of intact complex I from Neurospora crassa, obtained from detergent-solubilised material (single particles). The L shape of the enzyme was established six years earlier [50], but the three-dimensional structures of the membrane domain and matrix domain were determined separately using two-dimensional crystals. Thus, in the earlier work, it was not clear how these two domains would fit together to form the whole complex. Furthermore, Guénebaut et al. determined the location of the 49 kDa subunit using immunolabelling. This is the first direct evidence for the location of a subunit within the three-dimensional structure of complex I to be presented
    • Guénebaut V, Vincentelli R, Mills D, Weiss H, Leonard KR: Three dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction. J Mol Biol 1997, 265:409-418. The authors present the first three-dimensional structure of intact complex I from Neurospora crassa, obtained from detergent-solubilised material (single particles). The L shape of the enzyme was established six years earlier [50], but the three-dimensional structures of the membrane domain and matrix domain were determined separately using two-dimensional crystals. Thus, in the earlier work, it was not clear how these two domains would fit together to form the whole complex. Furthermore, Guénebaut et al. determined the location of the 49 kDa subunit using immunolabelling. This is the first direct evidence for the location of a subunit within the three-dimensional structure of complex I to be presented.
    • (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
  • 44
    • 0032512616 scopus 로고    scopus 로고
    • Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • The authors show the first three-dimensional structure of complex I from Escherichia coli. They established that the structure of the E. coli enzyme is consistent with that of the Neurospora crassa enzyme, even though the latter has at least 21 more subunits. Both structures were determined essentially the same way as the structure of N. crassa complex I one year earlier [43••]
    • Guénebaut V, Schutt A, Weiss H, Leonard K, Friedrich T: consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I). J Mol Biol 1998, 276:105-112. The authors show the first three-dimensional structure of complex I from Escherichia coli. They established that the structure of the E. coli enzyme is consistent with that of the Neurospora crassa enzyme, even though the latter has at least 21 more subunits. Both structures were determined essentially the same way as the structure of N. crassa complex I one year earlier [43••].
    • (1998) J Mol Biol , vol.276 , pp. 105-112
    • Guénebaut, V.1    Schutt, A.2    Weiss, H.3    Leonard, K.4    Friedrich, T.5
  • 45
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice
    • The author presents the first three-dimensional structure of bovine complex I. The resolution of 22 Å, obtained using electron cryomicroscopy, represents currently the highest resolution for the structure of complex I. The structure reveals for the first time a narrowing between the membrane domain and the matrix domain (the stalk). The stalk is interesting because it may indicate the locations of one of the iron-sulfur clusters (N-2) and a nearby ubiquinone-binding site (see text)
    • Grigorieff N: Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice. J Mol Biol 1998, 277:1033-1046. The author presents the first three-dimensional structure of bovine complex I. The resolution of 22 Å, obtained using electron cryomicroscopy, represents currently the highest resolution for the structure of complex I. The structure reveals for the first time a narrowing between the membrane domain and the matrix domain (the stalk). The stalk is interesting because it may indicate the locations of one of the iron-sulfur clusters (N-2) and a nearby ubiquinone-binding site (see text).
    • (1998) J Mol Biol , vol.277 , pp. 1033-1046
    • Grigorieff, N.1
  • 46
    • 0026472383 scopus 로고
    • Resolution of NADH-ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme
    • Finel M, Skehel JM, Albracht SPJ, Fearnley IM, Walker JE: Resolution of NADH-ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme. Biochemistry 1992, 31:11425-11434.
    • (1992) Biochemistry , vol.31 , pp. 11425-11434
    • Finel, M.1    Skehel, J.M.2    Albracht, S.P.J.3    Fearnley, I.M.4    Walker, J.E.5
  • 47
    • 0024635450 scopus 로고
    • A small isoform of NADH:ubiquinone oxidoreductase (complex I) without mitochondrially encoded subunits is made in chloramphenicol-treated Neurospora crassa
    • Friedrich T, Hofhaus G, Ise W, Nehls U, Schmilz B, Weiss H: A small isoform of NADH:ubiquinone oxidoreductase (complex I) without mitochondrially encoded subunits is made in chloramphenicol-treated Neurospora crassa. Eur J Biochem 1989, 180:173-180.
    • (1989) Eur J Biochem , vol.180 , pp. 173-180
    • Friedrich, T.1    Hofhaus, G.2    Ise, W.3    Nehls, U.4    Schmilz, B.5    Weiss, H.6
  • 48
    • 0027290826 scopus 로고
    • NADH-quinone oxidoreductase, the most complex complex
    • Ohnishi T: NADH-quinone oxidoreductase, the most complex complex. J Bioenerg Biomembr 1993, 25:325-329.
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 325-329
    • Ohnishi, T.1
  • 49
    • 0031033436 scopus 로고    scopus 로고
    • Proton-translocation by membrane-bound NADH:ubiquinone-oxidoreductase (complex I) through redoxgated ligand conduction
    • Brandt U: Proton-translocation by membrane-bound NADH:ubiquinone-oxidoreductase (complex I) through redoxgated ligand conduction. Biochim Biophys Acta 1997, 1318:79-91.
    • (1997) Biochim Biophys Acta , vol.1318 , pp. 79-91
    • Brandt, U.1
  • 50
    • 0026077298 scopus 로고
    • Electron-microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex-I)
    • Hofhaus G, Weiss H, Leonard K: Electron-microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex-I). J Mol Biol 1991, 221:1027-1043.
    • (1991) J Mol Biol , vol.221 , pp. 1027-1043
    • Hofhaus, G.1    Weiss, H.2    Leonard, K.3
  • 51
    • 0016299061 scopus 로고
    • Electron microscopy of the stacked disk aggregate of tobacco mosaic virus protein II. The influence of electron irradiation on the stain distribution
    • Unwin PNT: Electron microscopy of the stacked disk aggregate of tobacco mosaic virus protein II. The influence of electron irradiation on the stain distribution. J Mol Biol 1974, 87:657-670.
    • (1974) J Mol Biol , vol.87 , pp. 657-670
    • Unwin, P.N.T.1
  • 52
    • 0016296364 scopus 로고
    • Electron microscopy of the stacked disk aggregate of tobacco mosaic virus protein I. Three-dimensional image reconstruction
    • Unwin PNT, Klug A: Electron microscopy of the stacked disk aggregate of tobacco mosaic virus protein I. Three-dimensional image reconstruction. J Mol Biol 1974, 87:641-656.
    • (1974) J Mol Biol , vol.87 , pp. 641-656
    • Unwin, P.N.T.1    Klug, A.2
  • 54
    • 0029817347 scopus 로고    scopus 로고
    • Large-scale chromatographic purification of F1F0-ATPase and complex I from bovine heart mitochondria
    • Buchanan SK, Walker JE: Large-scale chromatographic purification of F1F0-ATPase and complex I from bovine heart mitochondria. Biochem J 1996, 318:343-349.
    • (1996) Biochem J , vol.318 , pp. 343-349
    • Buchanan, S.K.1    Walker, J.E.2
  • 55
    • 0025979241 scopus 로고
    • cDNA and genomic DNA-sequence of the 21.3 kDa subunit of NADH-ubiquinone reductase (complex I) from Neurospora crassa
    • Nehls U, Hemmer S, Röhlen DA, Van der Pas JC, Preis D, Sackmann U, Weiss H: cDNA and genomic DNA-sequence of the 21.3 kDa subunit of NADH-ubiquinone reductase (complex I) from Neurospora crassa. Biochim Biophys Acta 1991, 1088:325-326.
    • (1991) Biochim Biophys Acta , vol.1088 , pp. 325-326
    • Nehls, U.1    Hemmer, S.2    Röhlen, D.A.3    Van Der Pas, J.C.4    Preis, D.5    Sackmann, U.6    Weiss, H.7
  • 56
    • 0026496312 scopus 로고
    • Primary structure and mitochondrial import in vitro of the 20.9-kDa subunit of complex I from Neurospora crassa
    • Azevedo JE, Nehls U, Eckerskorn C, Heinrich H, Rothe H, Weiss H, Werner S: Primary structure and mitochondrial import in vitro of the 20.9-kDa subunit of complex I from Neurospora crassa. Biochem J 1992, 288:29-34.
    • (1992) Biochem J , vol.288 , pp. 29-34
    • Azevedo, J.E.1    Nehls, U.2    Eckerskorn, C.3    Heinrich, H.4    Rothe, H.5    Weiss, H.6    Werner, S.7
  • 57
    • 0027191017 scopus 로고
    • The 12.3 kDa subunit of complex I (respiratory chain NADH dehydrogenase) from Neurospora crassa - cDNA cloning and chromosomal mapping of the gene
    • Videira A, Azevedo JE, Werner S, Cabral P: The 12.3 kDa subunit of complex I (respiratory chain NADH dehydrogenase) from Neurospora crassa - cDNA cloning and chromosomal mapping of the gene. Biochem J 1993, 291:729-732.
    • (1993) Biochem J , vol.291 , pp. 729-732
    • Videira, A.1    Azevedo, J.E.2    Werner, S.3    Cabral, P.4
  • 58
    • 0028178325 scopus 로고
    • Characterization of a membrane fragment of respiratory chain complex I from Neurospora crassa - Insights on the topology of the ubiquinone-binding site
    • Azevedo JE, Videira A: Characterization of a membrane fragment of respiratory chain complex I from Neurospora crassa - Insights on the topology of the ubiquinone-binding site. Int J Biochem 1994, 26:505-510.
    • (1994) Int J Biochem , vol.26 , pp. 505-510
    • Azevedo, J.E.1    Videira, A.2
  • 59
    • 0025738723 scopus 로고
    • NADH-ubiquinone oxidoreductase from bovine heart mitochondria - cDNA sequences of the import precursors of the nuclear-encoded 39 kDa and 42 kDa subunits
    • Fearnley IM, Finel M, Skehel JM, Walker JE: NADH-ubiquinone oxidoreductase from bovine heart mitochondria - cDNA sequences of the import precursors of the nuclear-encoded 39 kDa and 42 kDa subunits. Biochem J 1991, 278:821-829.
    • (1991) Biochem J , vol.278 , pp. 821-829
    • Fearnley, I.M.1    Finel, M.2    Skehel, J.M.3    Walker, J.E.4
  • 60
    • 0004177528 scopus 로고    scopus 로고
    • Outline of theory of protein electron transfer
    • Edited by Bendall DS. Oxford: BIOS Scientific Publishers Ltd
    • Moser CC, Dutton PL: Outline of theory of protein electron transfer. In Protein Electron Transfer. Edited by Bendall DS. Oxford: BIOS Scientific Publishers Ltd; 1996:1-21.
    • (1996) Protein Electron Transfer , pp. 1-21
    • Moser, C.C.1    Dutton, P.L.2
  • 62
    • 0031042359 scopus 로고    scopus 로고
    • Proton pumping of mitochondrial complex I: Differential activation by analogs of ubiquinone
    • Helfenbaum L, Ngo A, Ghelli A, Linnane AW, Esposti MD: Proton pumping of mitochondrial complex I: Differential activation by analogs of ubiquinone. J Bioenerg Biomembr 1997, 29:71-80.
    • (1997) J Bioenerg Biomembr , vol.29 , pp. 71-80
    • Helfenbaum, L.1    Ngo, A.2    Ghelli, A.3    Linnane, A.W.4    Esposti, M.D.5
  • 63
    • 0031010114 scopus 로고    scopus 로고
    • Probing the ubiquinone reduction site of mitochondrial complex I using novel cationic inhibitors
    • Miyoshi H, Inoue M, Okamoto S, Ohshima M, Sakamoto K, Iwamura H: Probing the ubiquinone reduction site of mitochondrial complex I using novel cationic inhibitors. J Biol Chem 1997, 272:16176-16183.
    • (1997) J Biol Chem , vol.272 , pp. 16176-16183
    • Miyoshi, H.1    Inoue, M.2    Okamoto, S.3    Ohshima, M.4    Sakamoto, K.5    Iwamura, H.6
  • 65
    • 0032551770 scopus 로고    scopus 로고
    • Essential structural factors of annonaceous acetogenins as potent inhibitors of mitochondrial complex I
    • Miyoshi H, Ohshima M, Shimada H, Akagi T, Iwamura H, McLaughlin JL: Essential structural factors of annonaceous acetogenins as potent inhibitors of mitochondrial complex I. Biochim Biophys Acta 1998, 1365:443-452.
    • (1998) Biochim Biophys Acta , vol.1365 , pp. 443-452
    • Miyoshi, H.1    Ohshima, M.2    Shimada, H.3    Akagi, T.4    Iwamura, H.5    McLaughlin, J.L.6
  • 66
    • 0032485883 scopus 로고    scopus 로고
    • Characterization of the ubiquinone reduction site of mitochondrial complex I using bulky synthetic ubiquinones
    • Ohshima M, Miyoshi H, Sakamoto K, Takegami K, Iwata J, Kuwabara K, Iwamura H, Yagi T: Characterization of the ubiquinone reduction site of mitochondrial complex I using bulky synthetic ubiquinones. Biochemistry 1998, 37:6436-6445.
    • (1998) Biochemistry , vol.37 , pp. 6436-6445
    • Ohshima, M.1    Miyoshi, H.2    Sakamoto, K.3    Takegami, K.4    Iwata, J.5    Kuwabara, K.6    Iwamura, H.7    Yagi, T.8
  • 67
    • 0344820721 scopus 로고    scopus 로고
    • Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase)
    • Okun JG, Lummen P, Brandt U: Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH: ubiquinone oxidoreductase). J Biol Chem 1999, 274:2625-2630.
    • (1999) J Biol Chem , vol.274 , pp. 2625-2630
    • Okun, J.G.1    Lummen, P.2    Brandt, U.3
  • 68
    • 0032573198 scopus 로고    scopus 로고
    • Role of the isoprenyl tail of ubiquinone in reaction with respiratory enzymes: Studies with bovine heart mitochondrial complex I and Escherichia coli bo-type ubiquinol oxidase
    • Sakamoto K, Miyoshi H, Ohshima M, Kuwabara K, Kano K, Akagi T, Mogi T, Iwamura H: Role of the isoprenyl tail of ubiquinone in reaction with respiratory enzymes: Studies with bovine heart mitochondrial complex I and Escherichia coli bo-type ubiquinol oxidase. Biochemistry 1998, 37:15106-15113.
    • (1998) Biochemistry , vol.37 , pp. 15106-15113
    • Sakamoto, K.1    Miyoshi, H.2    Ohshima, M.3    Kuwabara, K.4    Kano, K.5    Akagi, T.6    Mogi, T.7    Iwamura, H.8
  • 69
    • 0032490102 scopus 로고    scopus 로고
    • Quinone specificity of complex I
    • Lenaz G: Quinone specificity of complex I. Biochim Biophys Acta 1998, 1364:207-221.
    • (1998) Biochim Biophys Acta , vol.1364 , pp. 207-221
    • Lenaz, G.1
  • 70
    • 0032490114 scopus 로고    scopus 로고
    • Inhibitors of NADH-ubiquinone reductase: An overview
    • Esposti MD: Inhibitors of NADH-ubiquinone reductase: An overview. Biochim Biophys Acta 1998, 1364:222-235.
    • (1998) Biochim Biophys Acta , vol.1364 , pp. 222-235
    • Esposti, M.D.1
  • 71
    • 0021099044 scopus 로고
    • Evidence of an ubisemiquinone radical(s) from the NADH-ubiquinone reductase of the mitochondrial respiratory chain
    • Suzuki H, King TE: Evidence of an ubisemiquinone radical(s) from the NADH-ubiquinone reductase of the mitochondrial respiratory chain. J Biol Chem 1983, 258:352-358.
    • (1983) J Biol Chem , vol.258 , pp. 352-358
    • Suzuki, H.1    King, T.E.2
  • 72
    • 0025078650 scopus 로고
    • Structure and function of an archetypal respiratory chain complex - NADH ubiquinone reductase
    • Ragan CI: Structure and function of an archetypal respiratory chain complex - NADH ubiquinone reductase. Biochem Soc Trans 1990, 18:515-516.
    • (1990) Biochem Soc Trans , vol.18 , pp. 515-516
    • Ragan, C.I.1
  • 73
    • 0027185319 scopus 로고
    • Kinetics, control, and mechanism of ubiquinone reduction by the mammalian respiratory chain-linked NADH-ubiquinone reductase
    • Vinogradov AD: Kinetics, control, and mechanism of ubiquinone reduction by the mammalian respiratory chain-linked NADH-ubiquinone reductase. J Bioenerg Biomembr 1993, 25:367-375.
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 367-375
    • Vinogradov, A.D.1
  • 74
    • 0028023673 scopus 로고
    • The mechanism of proton and electron-transport in mitochondrial complex I
    • Esposti MD, Ghelli A: The mechanism of proton and electron-transport in mitochondrial complex I. Biochim Biophys Acta 1994, 1187:116-120.
    • (1994) Biochim Biophys Acta , vol.1187 , pp. 116-120
    • Esposti, M.D.1    Ghelli, A.2
  • 76
    • 0032311426 scopus 로고    scopus 로고
    • Structure-function studies of iron-sulfur clusters and semiquinones in the NADH-Q oxidoreductase segment of the respiratory chain
    • Ohnishi T, Sled VD, Yano T, Yagi T, Burbaev DS, Vinogradov AD: Structure-function studies of iron-sulfur clusters and semiquinones in the NADH-Q oxidoreductase segment of the respiratory chain. Biochim Biophys Acta 1998, 1365:301-308.
    • (1998) Biochim Biophys Acta , vol.1365 , pp. 301-308
    • Ohnishi, T.1    Sled, V.D.2    Yano, T.3    Yagi, T.4    Burbaev, D.S.5    Vinogradov, A.D.6
  • 77
    • 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
    • Van Belzen R, Kotlyar AB, Moon N, Dunham WR, Albracht SPJ: The iron-sulfur clusters 2 and ubisemiquinone radicals of NADH:ubiquinone oxidoreductase are involved in energy coupling in submitochondrial particles. Biochemistry 1997, 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
  • 78
    • 0031027369 scopus 로고    scopus 로고
    • Bovine-heart NADH:ubiquinone oxidoreductase is a monomer with 8 Fe-S clusters and 2 FMN groups
    • Albracht SPJ, MAriette A, de Jong P: Bovine-heart NADH:ubiquinone oxidoreductase is a monomer with 8 Fe-S clusters and 2 FMN groups. Biochim Biophys Acta 1997, 1318:92-106.
    • (1997) Biochim Biophys Acta , vol.1318 , pp. 92-106
    • Albracht, S.P.J.1    Mariette, A.2    De Jong, P.3
  • 79
    • 0032321581 scopus 로고    scopus 로고
    • Comparison of energization of complex I in membrane particles from Paracoccus denitrificans and bovine heart mitochondria
    • Kotlyar AB, Albracht SPJ, Van Spanning RJM: Comparison of energization of complex I in membrane particles from Paracoccus denitrificans and bovine heart mitochondria. Biochim Biophys Acta 1998, 1365:53-59.
    • (1998) Biochim Biophys Acta , vol.1365 , pp. 53-59
    • Kotlyar, A.B.1    Albracht, S.P.J.2    Van Spanning, R.J.M.3
  • 80
    • 0031574275 scopus 로고    scopus 로고
    • Identification of the TYKY homologous subunit of complex I from Neurospora crassa
    • Duarte M, Schulte U, Videira A: Identification of the TYKY homologous subunit of complex I from Neurospora crassa. Biochim Biophys Acta 1997, 1322:237-241.
    • (1997) Biochim Biophys Acta , vol.1322 , pp. 237-241
    • Duarte, M.1    Schulte, U.2    Videira, A.3
  • 81
    • 0032490117 scopus 로고    scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    • Friedrich T: The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochim Biophys Acta 1998, 1364:134-146.
    • (1998) Biochim Biophys Acta , vol.1364 , pp. 134-146
    • Friedrich, T.1
  • 82
    • 0029988718 scopus 로고    scopus 로고
    • Comparison of the structural features of ubiquinone reduction sites between glucose dehydrogenase in Escherichia coli and bovine heart mitochondrial complex I
    • Sakamoto K, Miyoshi H, Matsushita K, Nakagawa M, Ikeda J, Ohshima M, Adachi O, Akagi T, Iwamura H: Comparison of the structural features of ubiquinone reduction sites between glucose dehydrogenase in Escherichia coli and bovine heart mitochondrial complex I. Eur J Biochem 1996, 237:128-135.
    • (1996) Eur J Biochem , vol.237 , pp. 128-135
    • Sakamoto, K.1    Miyoshi, H.2    Matsushita, K.3    Nakagawa, M.4    Ikeda, J.5    Ohshima, M.6    Adachi, O.7    Akagi, T.8    Iwamura, H.9
  • 83
    • 0016754421 scopus 로고
    • The protonmotive Q cycle: A general formulation
    • Mitchell P: The protonmotive Q cycle: A general formulation. FEBS Lett 1975, 59:137-139.
    • (1975) FEBS Lett , vol.59 , pp. 137-139
    • Mitchell, P.1
  • 84
    • 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
    • Darrouzet E, Issartel JP, Lunardi J, Dupuis A: 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 998, 431:34-38.
    • (1998) FEBS Lett , vol.431 , pp. 34-38
    • Darrouzet, E.1    Issartel, J.P.2    Lunardi, J.3    Dupuis, A.4
  • 85
    • 0025886958 scopus 로고
    • Primary structures of 2 subunits of NADH-ubiquinone reductase from Neurospora crassa concerned with NADH oxidation - Relationship to a soluble NAD-reducing hydrogenase of Alcaligenes eutrophus
    • Preis D, Weidner U, Conzen C, Azevedo JE, Nehls U, Röhlen D, Van der Pas J, Sackmann U, Schneider R, Werner S, Weiss H: Primary structures of 2 subunits of NADH-ubiquinone reductase from Neurospora crassa concerned with NADH oxidation - Relationship to a soluble NAD-reducing hydrogenase of Alcaligenes eutrophus. Biochim Biophys Acta 1991, 1090:133-138.
    • (1991) Biochim Biophys Acta , vol.1090 , pp. 133-138
    • Preis, D.1    Weidner, U.2    Conzen, C.3    Azevedo, J.E.4    Nehls, U.5    Röhlen, D.6    Van Der Pas, J.7    Sackmann, U.8    Schneider, R.9    Werner, S.10    Weiss, H.11
  • 86
    • 0024350374 scopus 로고
    • Mitochondrial NADH-ubiquinone reductase - Complementary-DNA sequence of the import precursor of the bovine 75-kDa subunit
    • Runswick MJ, Gennis RB, Fearnley IM, Walker JE: Mitochondrial NADH-ubiquinone reductase - Complementary-DNA sequence of the import precursor of the bovine 75-kDa subunit. Biochemistry 1989, 28:9452-9459.
    • (1989) Biochemistry , vol.28 , pp. 9452-9459
    • Runswick, M.J.1    Gennis, R.B.2    Fearnley, I.M.3    Walker, J.E.4
  • 87
    • 0026032458 scopus 로고
    • Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase
    • Pilkington SJ, Skehel JM, Gennis RB, Walker JE: Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase. Biochemistry 1991, 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
  • 88
    • 0025364847 scopus 로고
    • The 49-kDa subunit of NADH-ubiquinone reductase (complex I) from Neurospora crassa mitochondria - Primary structure of the gene and the protein
    • Preis D, Van der Pas JC, Nehls U, Röhlen DA, Sackmann U, Jahnke U, Weiss H: The 49-kDa subunit of NADH-ubiquinone reductase (complex I) from Neurospora crassa mitochondria - Primary structure of the gene and the protein. Curr Genet 1990, 18:59-64.
    • (1990) Curr Genet , vol.18 , pp. 59-64
    • Preis, D.1    Van Der Pas, J.C.2    Nehls, U.3    Röhlen, D.A.4    Sackmann, U.5    Jahnke, U.6    Weiss, H.7
  • 89
    • 0024634879 scopus 로고
    • A homolog of the nuclear coded 49 kDa subunit of bovine mitochondrial NADH-ubiquinone reductase is coded in chloroplast DNA
    • Fearnley IM, Runswick MJ, Walker JE: A homolog of the nuclear coded 49 kDa subunit of bovine mitochondrial NADH-ubiquinone reductase is coded in chloroplast DNA. EMBO J 1989, 8:665-672.
    • (1989) EMBO J , vol.8 , pp. 665-672
    • Fearnley, I.M.1    Runswick, M.J.2    Walker, J.E.3
  • 90
    • 0026074244 scopus 로고
    • Relationship between a subunit of NADH dehydrogenase (complex I) and a protein family including subunits of cytochrome reductase and processing protease of mitochondria
    • Röhlen DA, Hoffmann J, Van der Pas JC, Nehls U, Preis D, Sackmann U, Weiss H: Relationship between a subunit of NADH dehydrogenase (complex I) and a protein family including subunits of cytochrome reductase and processing protease of mitochondria. FEBS Lett 1991, 278:75-78.
    • (1991) FEBS Lett , vol.278 , pp. 75-78
    • Röhlen, D.A.1    Hoffmann, J.2    Van Der Pas, J.C.3    Nehls, U.4    Preis, D.5    Sackmann, U.6    Weiss, H.7
  • 91
    • 0025145496 scopus 로고
    • Primary structure and expression of a nuclear-coded subunit of complex I homologous to proteins specified by the chloroplast genome
    • Videira A, Tropschüg M, Werner S: Primary structure and expression of a nuclear-coded subunit of complex I homologous to proteins specified by the chloroplast genome. Biochem Biophys Res Commun 1990, 171:1168-1174.
    • (1990) Biochem Biophys Res Commun , vol.171 , pp. 1168-1174
    • Videira, A.1    Tropschüg, M.2    Werner, S.3
  • 92
    • 0025805272 scopus 로고
    • The 30 kDa subunit of bovine mitochondrial complex I is homologous to a protein coded in chloroplast DNA
    • Pilkington SJ, Skehel JM, Walker JE: The 30 kDa subunit of bovine mitochondrial complex I is homologous to a protein coded in chloroplast DNA. Biochemistry 1991, 30:1901-1908.
    • (1991) Biochemistry , vol.30 , pp. 1901-1908
    • Pilkington, S.J.1    Skehel, J.M.2    Walker, J.E.3
  • 93
    • 0028132103 scopus 로고
    • Complementary-DNA sequences of the 24-kDa and 21-kDa subunits of complex I from Neurospora
    • Azevedo JE, Duarte M, Belo JA. Werner S, Videira A: Complementary-DNA sequences of the 24-kDa and 21-kDa subunits of complex I from Neurospora. Biochim Biophys Acta 1994, 1188:159-161.
    • (1994) Biochim Biophys Acta , vol.1188 , pp. 159-161
    • Azevedo, J.E.1    Duarte, M.2    Belo, J.A.3    Werner, S.4    Videira, A.5
  • 94
    • 0024559488 scopus 로고
    • Mitochondrial NADH-ubiquinone reductase: Complementary DNA sequence of import precursor of bovine and human 24 kDa subunit
    • Pilkington SJ, Walker JE: Mitochondrial NADH-ubiquinone reductase: Complementary DNA sequence of import precursor of bovine and human 24 kDa subunit. Biochemistry 1989, 28:3257-3264.
    • (1989) Biochemistry , vol.28 , pp. 3257-3264
    • Pilkington, S.J.1    Walker, J.E.2
  • 95
    • 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
    • Walker JE, Arizmendi JM, Dupuis A. Fearnley IM, Finel M, Medd SM, Pilkington SJ, Runswick MJ, Skehel JM: 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 1992, 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
  • 96
    • 0000432497 scopus 로고    scopus 로고
    • Primary structure of a ferredoxin-like iron-sulfur subunit of complex I from Neurospora crassa
    • Duarte M, Finel M. Videira A: Primary structure of a ferredoxin-like iron-sulfur subunit of complex I from Neurospora crassa. Biochim Biophys Acta 1996, 1275:151-153.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 151-153
    • Duarte, M.1    Finel, M.2    Videira, A.3
  • 97
    • 0025854234 scopus 로고
    • A homolog of a nuclear-coded iron sulfur protein subunit of bovine mitochondrial complex I is encoded in chloroplast genomes
    • Dupuis A, Skehel JM, Walker JE: A homolog of a nuclear-coded iron sulfur protein subunit of bovine mitochondrial complex I is encoded in chloroplast genomes. Biochemistry 1991, 30:2954-2960.
    • (1991) Biochemistry , vol.30 , pp. 2954-2960
    • Dupuis, A.1    Skehel, J.M.2    Walker, J.E.3
  • 98
    • 0028936592 scopus 로고
    • Inactivation of genes encoding subunits of the peripheral and membrane arms of Neurospora mitochondrial complex I and effects on enzyme assembly
    • Duarte M, Sousa R, Videira A: Inactivation of genes encoding subunits of the peripheral and membrane arms of Neurospora mitochondrial complex I and effects on enzyme assembly. Genetics 1995, 139:1211-1221.
    • (1995) Genetics , vol.139 , pp. 1211-1221
    • Duarte, M.1    Sousa, R.2    Videira, A.3
  • 99
    • 0026517071 scopus 로고
    • NADH-ubiquinone oxidoreductase from bovine heart mitochondria - A 4th nuclear encoded subunit with a homolog encoded in chloroplast genomes
    • Arizmendi JM, Runswick MJ, Skehel JM, Walker JE: NADH-ubiquinone oxidoreductase from bovine heart mitochondria - A 4th nuclear encoded subunit with a homolog encoded in chloroplast genomes. FEBS Lett 1992, 301:237-242.
    • (1992) FEBS Lett , vol.301 , pp. 237-242
    • Arizmendi, J.M.1    Runswick, M.J.2    Skehel, J.M.3    Walker, J.E.4
  • 100
    • 0025309621 scopus 로고
    • Molecular-cloning of subunits of complex I from Neurospora crassa - Primary structure and in vitro expression of a 22-kDa polypeptide
    • Videira A, Tropschüg M, Wachter E, Schneider H, Werner S: Molecular-cloning of subunits of complex I from Neurospora crassa - Primary structure and in vitro expression of a 22-kDa polypeptide. J Biol Chem 1990, 265:13060-13065.
    • (1990) J Biol Chem , vol.265 , pp. 13060-13065
    • Videira, A.1    Tropschüg, M.2    Wachter, E.3    Schneider, H.4    Werner, S.5
  • 101
    • 0025915639 scopus 로고
    • NADH-ubiquinore oxidoreductase from bovine mitochondria - cDNA sequence of a 19-kDa cysteine-rich subunit
    • Dupuis A, Skehel JM, Walker JE: NADH-ubiquinore oxidoreductase from bovine mitochondria - cDNA sequence of a 19-kDa cysteine-rich subunit. Biochem J 1991, 277:11-15.
    • (1991) Biochem J , vol.277 , pp. 11-15
    • Dupuis, A.1    Skehel, J.M.2    Walker, J.E.3
  • 102
    • 0025860648 scopus 로고
    • Primary structure of the nuclear-encoded 18.3 kDa subunit of NADH-ubiquinone reductase (complex I) from Neurospora crassa mitochondria
    • Weidner U, Sackmann U, Nehls U, Weiss H: Primary structure of the nuclear-encoded 18.3 kDa subunit of NADH-ubiquinone reductase (complex I) from Neurospora crassa mitochondria. Biochim Biophys Acta 1991, 1089:391-392.
    • (1991) Biochim Biophys Acta , vol.1089 , pp. 391-392
    • Weidner, U.1    Sackmann, U.2    Nehls, U.3    Weiss, H.4
  • 103
    • 0028204481 scopus 로고
    • In organello assembly of respiratory chain complex I - Primary structure of the 14.8 kDa subunit of Neurospora crassa complex
    • Azevedo JE, Eckerskorn C, Werner S: In organello assembly of respiratory chain complex I - Primary structure of the 14.8 kDa subunit of Neurospora crassa complex. Biochem J 1994, 299:297-302.
    • (1994) Biochem J , vol.299 , pp. 297-302
    • Azevedo, J.E.1    Eckerskorn, C.2    Werner, S.3
  • 104
    • 0026473063 scopus 로고
    • Complementary-DNA sequences of 2 14.5 kDa subunits of NADH-ubiquinone oxidoreductase from bovine heart mitochondria - Completion of the primary structure of the complex
    • Arizmendi JM, Skehel JM, Runswick MJ, Fearnley IM, Walker JE: Complementary-DNA sequences of 2 14.5 kDa subunits of NADH-ubiquinone oxidoreductase from bovine heart mitochondria - Completion of the primary structure of the complex. FEBS Lett 1992, 313:80-84.
    • (1992) FEBS Lett , vol.313 , pp. 80-84
    • Arizmendi, J.M.1    Skehel, J.M.2    Runswick, M.J.3    Fearnley, I.M.4    Walker, J.E.5
  • 105
    • 0025767804 scopus 로고
    • Primary structure of the nuclear-encoded 29.9 kDa subunit of NADH-ubiquinone reductase from Neurospora crassa mitochondria
    • Van der Pas JC, Röhlen DA, Weidner U, Weiss H: Primary structure of the nuclear-encoded 29.9 kDa subunit of NADH-ubiquinone reductase from Neurospora crassa mitochondria. Biochim Biophys Acta 1991, 1089:389-390.
    • (1991) Biochim Biophys Acta , vol.1089 , pp. 389-390
    • Van Der Pas, J.C.1    Röhlen, D.A.2    Weidner, U.3    Weiss, H.4
  • 106
    • 0027528847 scopus 로고
    • Primary structure of the nuclear-encoded 10.5-kDa subunit of complex I from Neurospora crassa
    • Duarte M, Belo JA, Videira A: Primary structure of the nuclear-encoded 10.5-kDa subunit of complex I from Neurospora crassa. Biochim Biophys Acta 1993, 1172:327-328.
    • (1993) Biochim Biophys Acta , vol.1172 , pp. 327-328
    • Duarte, M.1    Belo, J.A.2    Videira, A.3
  • 107
    • 0025779382 scopus 로고
    • The acyl-carrier protein in Neurospora crassa mitochondria is a subunit of NADH-ubiquinone reductase (complex I)
    • Sackmann U, Zensen R. Röhlen D, Jahnke U, Weiss H: The acyl-carrier protein in Neurospora crassa mitochondria is a subunit of NADH-ubiquinone reductase (complex I). Eur J Biochem 1991, 200:463-469.
    • (1991) Eur J Biochem , vol.200 , pp. 463-469
    • Sackmann, U.1    Zensen, R.2    Röhlen, D.3    Jahnke, U.4    Weiss, H.5
  • 108
    • 0025827137 scopus 로고
    • Presence of an acyl carrier protein in NADH-ubiquinone oxidoreductase from bovine heart mitochondria
    • Runswick MJ, Fearnley IM, Skehel JM, Walker JE: Presence of an acyl carrier protein in NADH-ubiquinone oxidoreductase from bovine heart mitochondria. FEBS Lett 1991, 286:121-124.
    • (1991) FEBS Lett , vol.286 , pp. 121-124
    • Runswick, M.J.1    Fearnley, I.M.2    Skehel, J.M.3    Walker, J.E.4
  • 109
    • 0025755811 scopus 로고
    • NADH-ubiquinone oxidoreductase from bovine heart mitochondria - Complementary-DNA sequence of the import precursor of the 10 kDa subunit of the flavoprotein fragment
    • Skehel JM, Pilkington SJ, Runswick MJ, Fearnley IM, Walker JE: NADH-ubiquinone oxidoreductase from bovine heart mitochondria - Complementary-DNA sequence of the import precursor of the 10 kDa subunit of the flavoprotein fragment. FEBS Lett 1991, 282:135-138.
    • (1991) FEBS Lett , vol.282 , pp. 135-138
    • Skehel, J.M.1    Pilkington, S.J.2    Runswick, M.J.3    Fearnley, I.M.4    Walker, J.E.5
  • 110
    • 0022402016 scopus 로고
    • The mitochondrial urf1 gene in Neurospora crassa has an intron that contains a novel type of urf
    • Burger G, Werner S: The mitochondrial urf1 gene in Neurospora crassa has an intron that contains a novel type of urf. J Mol Biol 1985, 186:231-242.
    • (1985) J Mol Biol , vol.186 , pp. 231-242
    • Burger, G.1    Werner, S.2
  • 112
    • 0022704076 scopus 로고
    • The E35 stopper mutant of Neurospora crassa - Precise localization of deletion end-points in mitochondrial-DNA and evidence that the deleted DNA codes for a subunit of NADH dehydrogenase
    • De Vries H, Alzner de Weerd B, Breitenberger CA, Chang DD, De Jonge JC, RajBhandary UL: The E35 stopper mutant of Neurospora crassa - Precise localization of deletion end-points in mitochondrial-DNA and evidence that the deleted DNA codes for a subunit of NADH dehydrogenase. EMBO J 1986, 5:779-785.
    • (1986) EMBO J , vol.5 , pp. 779-785
    • De Vries, H.1    Alzner De Weerd, B.2    Breitenberger, C.A.3    Chang, D.D.4    De Jonge, J.C.5    RajBhandary, U.L.6
  • 114
    • 0023138715 scopus 로고
    • Structure and expression of the overlapping ND4L and ND5 genes of Neurospora crassa mitochondria
    • Nelson MA, Macino G: Structure and expression of the overlapping ND4L and ND5 genes of Neurospora crassa mitochondria. Mol Gen Genet 1987, 206:307-317.
    • (1987) Mol Gen Genet , vol.206 , pp. 307-317
    • Nelson, M.A.1    Macino, G.2
  • 115
    • 0025295685 scopus 로고
    • Assembly of NADH:ubiquinone reductase (complex I) in Neurospora mitochondria - Independent pathways of nuclear-encoded and mitochondrially encoded subunits
    • Tuschen G, Sackmann U, Nehls U, Haiker H, Buse G, Weiss H: Assembly of NADH:ubiquinone reductase (complex I) in Neurospora mitochondria - Independent pathways of nuclear-encoded and mitochondrially encoded subunits. J Mol Biol 1990, 213:845-857.
    • (1990) J Mol Biol , vol.213 , pp. 845-857
    • Tuschen, G.1    Sackmann, U.2    Nehls, U.3    Haiker, H.4    Buse, G.5    Weiss, H.6


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