메뉴 건너뛰기




Volumn 43, Issue 12, 2004, Pages 3750-3755

Subunit Proximity in the H+-Translocating NADH-Quinone Oxidoreductase Probed by Zero-Length Cross-Linking

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CROSSLINKING; ESCHERICHIA COLI; ESTERS; TERNARY SYSTEMS;

EID: 1642392110     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049927s     Document Type: Article
Times cited : (37)

References (42)
  • 1
    • 0025760073 scopus 로고
    • The respiratory-chain NADH dehydrogenase (complex I) of mitochondria
    • Weiss, H., Friedrich, T., Hofhaus, G., and Preis, D. (1991) The respiratory-chain NADH dehydrogenase (complex I) of mitochondria, Eur. J. Biochem. 197, 563-576.
    • (1991) Eur. J. Biochem. , vol.197 , pp. 563-576
    • Weiss, H.1    Friedrich, T.2    Hofhaus, G.3    Preis, D.4
  • 2
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker, J. E. (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
  • 3
    • 0032490089 scopus 로고    scopus 로고
    • Iron-sulfur clusters semiquinones in Complex I
    • Ohnishi, T. (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
  • 4
    • 0037418550 scopus 로고    scopus 로고
    • The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: The secret unlocked
    • Yagi, T., and Matsuno-Yagi, A. (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
  • 5
    • 0032588194 scopus 로고    scopus 로고
    • +/2(e)over-bar stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles
    • +/2(e)over-bar 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
  • 6
    • 0038160473 scopus 로고    scopus 로고
    • Analysis of the subunit composition of complex I from bovine heart mitochondria
    • Carroll, J., Fearnley, I. M., Shannon, R. J., Hirst, J., and Walker, J. E. (2003) Analysis of the subunit composition of complex I from bovine heart mitochondria, Mol. Cell. Proteomics 2, 117-126.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 117-126
    • Carroll, J.1    Fearnley, I.M.2    Shannon, R.J.3    Hirst, J.4    Walker, J.E.5
  • 7
    • 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., and Matsuno-Yagi, A. (1993) Characteristics of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans as revealed by biochemical, biophysical, and molecular biological approaches, J. Bioenerg. Biomembr. 25, 339-345.
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 339-345
    • Yagi, T.1    Yano, T.2    Matsuno-Yagi, A.3
  • 9
    • 0032512616 scopus 로고    scopus 로고
    • Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Guénebaut, V., Schlitt, A., Weiss, H., Leonard, K., and Friedrich, T. (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
  • 10
    • 15844405973 scopus 로고    scopus 로고
    • Structural studies of the proton-translocating NADH-quinone oxidoreductase (NDH1) of Paracoccus denitrificans: Identity, property, and stoichiometry of the peripheral subunits
    • Takano, S., Yano, T., and Yagi, T. (1996) Structural studies of the proton-translocating NADH-quinone oxidoreductase (NDH1) of Paracoccus denitrificans: Identity, property, and stoichiometry of the peripheral subunits, Biochemistry 35, 9120-9127.
    • (1996) Biochemistry , vol.35 , pp. 9120-9127
    • Takano, S.1    Yano, T.2    Yagi, T.3
  • 11
    • 0033215393 scopus 로고    scopus 로고
    • +-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans: Studies on topology and stoichiometry of the peripheral subunits
    • +-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans: Studies on topology and stoichiometry of the peripheral subunits, J. Biol. Chem. 274, 28606-28611.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28606-28611
    • Yano, T.1    Yagi, T.2
  • 12
    • 0021866528 scopus 로고
    • Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase
    • Chomyn, A., Mariottini, P., Cleeter, M. W. J., Ragan, C. I., Matsuno-Yagi, A., Hatefi, Y., Doolittle, R. F., and Attardi, G. (1985) Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase, Nature 314, 591-597.
    • (1985) Nature , vol.314 , pp. 591-597
    • Chomyn, A.1    Mariottini, P.2    Cleeter, M.W.J.3    Ragan, C.I.4    Matsuno-Yagi, A.5    Hatefi, Y.6    Doolittle, R.F.7    Attardi, G.8
  • 13
    • 0023032242 scopus 로고
    • URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit
    • Chomyn, A., Cleeter, M. W. J., Ragan, C. I., Riley, M., Doolittle, R. F., and Attardi, G. (1986) URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit, Science 234, 614-618.
    • (1986) Science , vol.234 , pp. 614-618
    • Chomyn, A.1    Cleeter, M.W.J.2    Ragan, C.I.3    Riley, M.4    Doolittle, R.F.5    Attardi, G.6
  • 14
    • 0034773042 scopus 로고    scopus 로고
    • The origin of cluster N2 of the energy-transducing NADH-quinone oxidoreductase: Comparisons of phylogenetically related enzymes
    • Yano, T., and Ohnishi, T. (2001) The origin of cluster N2 of the energy-transducing NADH-quinone oxidoreductase: comparisons of phylogenetically related enzymes, J. Bioenerg. Biomembr. 33, 213-222.
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 213-222
    • Yano, T.1    Ohnishi, T.2
  • 15
    • 0037096980 scopus 로고    scopus 로고
    • Disruption of iron-sulphur cluster N2 from NADH: Ubiquinone oxidoreductase by site-directed mutagenesis
    • Duarte, M., Populo, H., Videira, A., Friedrich, T., and Schulte, U. (2002) Disruption of iron-sulphur cluster N2 from NADH: ubiquinone oxidoreductase by site-directed mutagenesis, Biochem. J. 364, 833-839.
    • (2002) Biochem. J. , vol.364 , pp. 833-839
    • Duarte, M.1    Populo, H.2    Videira, A.3    Friedrich, T.4    Schulte, U.5
  • 16
    • 0347481386 scopus 로고    scopus 로고
    • Iron-sulfur cluster N2 of the Escherichia coli NADH: Ubiquinone oxidoreductase (complex I) is located on subunit NuoB
    • Flemming, D., Schlitt, A., Spehr, V., Bischof, T., and Friedrich, T. (2003) Iron-sulfur cluster N2 of the Escherichia coli NADH: ubiquinone oxidoreductase (complex I) is located on subunit NuoB, J. Biol. Chem. 278, 47602-47609.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47602-47609
    • Flemming, D.1    Schlitt, A.2    Spehr, V.3    Bischof, T.4    Friedrich, T.5
  • 17
    • 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
    • Chevallet, M., Dupuis, A., Issartel, J. P., Lunardi, J., Van Belzen, R., and Albracht, S. P. (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.6
  • 19
    • 0035941007 scopus 로고    scopus 로고
    • +-translocating NADH-quinone oxidoreductase
    • +-translocating NADH-quinone oxidoreductase, FEBS Lett. 508, 385-388.
    • (2001) FEBS Lett. , vol.508 , pp. 385-388
    • Di Bernardo, S.1    Yagi, T.2
  • 20
    • 0037006973 scopus 로고    scopus 로고
    • Characterization of the membrane domain Nqo11 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Kao, M.-C., Di Bernardo, S., Matsuno-Yagi, A., and Yagi, T. (2002) Characterization of the membrane domain Nqo11 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans, Biochemistry, 41, 4377-4384.
    • (2002) Biochemistry , vol.41 , pp. 4377-4384
    • Kao, M.-C.1    Di Bernardo, S.2    Matsuno-Yagi, A.3    Yagi, T.4
  • 21
    • 0037461290 scopus 로고    scopus 로고
    • Characterization and topology of the membrane domain Nqo10 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Kao, M.-C., Di Bernardo, S., Matsuno-Yagi, A., and Yagi, T. (2003) Characterization and topology of the membrane domain Nqo10 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans, Biochemistry 42, 4534-4543.
    • (2003) Biochemistry , vol.42 , pp. 4534-4543
    • Kao, M.-C.1    Di Bernardo, S.2    Matsuno-Yagi, A.3    Yagi, T.4
  • 22
    • 0034622505 scopus 로고    scopus 로고
    • Exploring the membrane domain of the reduced nicotinamide adenine dinucleotide-quinone oxidoreductase of Paracoccus denitrificans: Characterization of the NQO7 subunit
    • Di Bernardo, S., Yano, T., and Yagi, T. (2000) Exploring the membrane domain of the reduced nicotinamide adenine dinucleotide-quinone oxidoreductase of Paracoccus denitrificans: Characterization of the NQO7 subunit, Biochemistry 39, 9411-9418.
    • (2000) Biochemistry , vol.39 , pp. 9411-9418
    • Di Bernardo, S.1    Yano, T.2    Yagi, T.3
  • 23
    • 0029112808 scopus 로고
    • Expression and characterization of the 66-kilodalton (NQO3) iron-sulfur subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Yano, T., Yagi, T., Sled', V. D., and Ohnishi, T. (1995) Expression and characterization of the 66-kilodalton (NQO3) iron-sulfur subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans, J. Biol. Chem. 270, 18264-18270.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18264-18270
    • Yano, T.1    Yagi, T.2    Sled', V.D.3    Ohnishi, T.4
  • 24
    • 0026686343 scopus 로고
    • Gene cluster of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans: Characterization of four structural gene products
    • Xu, X., Matsuno-Yagi, A., and Yagi, T. (1992) Gene cluster of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans: characterization of four structural gene products, Biochemistry 31, 6925-6932.
    • (1992) Biochemistry , vol.31 , pp. 6925-6932
    • Xu, X.1    Matsuno-Yagi, A.2    Yagi, T.3
  • 25
    • 0033215197 scopus 로고    scopus 로고
    • Characterization of the putative 2x[4Fe-4S] binding NQO9 subunit of the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans: Expression, reconstitution, and EPR characterization
    • Yano, T., Magnitsky, S., Sled', V. D., Ohnishi, T., and Yagi, T. (1999) Characterization of the putative 2x[4Fe-4S] binding NQO9 subunit of the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans: Expression, reconstitution, and EPR characterization, J. Biol. Chem. 274, 28598-28605.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28598-28605
    • Yano, T.1    Magnitsky, S.2    Sled', V.D.3    Ohnishi, T.4    Yagi, T.5
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0025358008 scopus 로고
    • Identification of the NADH-binding subunit of NADH-ubiquinone oxidoreductase of Paracoccus denitrificans
    • Yagi, T., and Dinh, T. M. (1990) Identification of the NADH-binding subunit of NADH-ubiquinone oxidoreductase of Paracoccus denitrificans, Biochemistry 29, 5515-5520.
    • (1990) Biochemistry , vol.29 , pp. 5515-5520
    • Yagi, T.1    Dinh, T.M.2
  • 28
    • 0025952505 scopus 로고
    • Characterization of the 25-kilodalton subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: Sequence similarity to the 24-kilodalton subunit of the flavoprotein fraction of mammalian complex I
    • Xu, X. M., Matsuno-Yagi, A., and Yagi, T. (1991) Characterization of the 25-kilodalton subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: sequence similarity to the 24-kilodalton subunit of the flavoprotein fraction of mammalian complex I, Biochemistry 30, 8678-8684.
    • (1991) Biochemistry , vol.30 , pp. 8678-8684
    • Xu, X.M.1    Matsuno-Yagi, A.2    Yagi, T.3
  • 29
    • 0025779257 scopus 로고
    • The NADH-binding subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: Gene cloning and deduced primary structure
    • Xu, X. M., Matsuno-Yagi, A., and Yagi, T. (1991) The NADH-binding subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: gene cloning and deduced primary structure, Biochemistry 30, 6422-6428.
    • (1991) Biochemistry , vol.30 , pp. 6422-6428
    • Xu, X.M.1    Matsuno-Yagi, A.2    Yagi, T.3
  • 30
    • 0028091327 scopus 로고
    • Expression of the 25 kilodalton iron-sulfur subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paraccocus denitrificans
    • Yano, T., Sled', V. D., Ohnishi, T., and Yagi, T. (1994) Expression of the 25 kilodalton iron-sulfur subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paraccocus denitrificans, Biochemistry 33, 494-499.
    • (1994) Biochemistry , vol.33 , pp. 494-499
    • Yano, T.1    Sled', V.D.2    Ohnishi, T.3    Yagi, T.4
  • 31
    • 0029864414 scopus 로고    scopus 로고
    • Expression and characterization of the flavoprotein subcomplex composed of 50-kDa (NQO1) and 25-kDa (NQO2) subunits of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Yano, T., Sled, V. D., Ohnishi, T., and Yagi, T. (1996) Expression and characterization of the flavoprotein subcomplex composed of 50-kDa (NQO1) and 25-kDa (NQO2) subunits of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans, J. Biol. Chem. 271, 5907-5913.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5907-5913
    • Yano, T.1    Sled, V.D.2    Ohnishi, T.3    Yagi, T.4
  • 32
    • 0025181840 scopus 로고
    • Zero-length crosslinking procedure with the use of active esters
    • Grabarek, Z., and Gergely, J. (1990) Zero-length crosslinking procedure with the use of active esters, Anal. Biochem. 185, 131-135.
    • (1990) Anal. Biochem. , vol.185 , pp. 131-135
    • Grabarek, Z.1    Gergely, J.2
  • 33
    • 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
    • Yano, T., Sklar, J., Nakamaru-Ogiso, E., Takahashi, Y., Yagi, T., and Ohnishi, T. (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
  • 34
    • 0027408368 scopus 로고
    • Mitochondrial NADH: Ubiquinone oxidoreductase (complex I): proximity of the subunits of the flavoprotein and the iron-sulfur protein subcomplexes
    • Yamaguchi, M., and Hatefi, Y. (1993) Mitochondrial NADH: ubiquinone oxidoreductase (complex I): proximity of the subunits of the flavoprotein and the iron-sulfur protein subcomplexes, Biochemistry 32, 1935-1939.
    • (1993) Biochemistry , vol.32 , pp. 1935-1939
    • Yamaguchi, M.1    Hatefi, Y.2
  • 35
    • 0037127215 scopus 로고    scopus 로고
    • 27C) in Nqo3 subunit in the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Thermus thermophilus HB-8
    • 27C) in Nqo3 subunit in the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Thermus thermophilus HB-8, J. Biol. Chem. 277, 1680-1688.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1680-1688
    • Nakamaru-Ogiso, E.1    Yano, T.2    Ohnishi, T.3    Yagi, T.4
  • 36
    • 0031592480 scopus 로고    scopus 로고
    • Three-dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction
    • Guénebaut, V., Vincentelli, R., Mills, D., Weiss, H., and Leonard, K. R. (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
  • 37
    • 0043208847 scopus 로고    scopus 로고
    • Functional implications from an unexpected position of the 49 kDa subunit of complex I
    • Zickermann, V., Bostina, M., Hunte, C., Ruiz, T., Radermacher, M., and Brandt, U. (2003) Functional implications from an unexpected position of the 49 kDa subunit of complex I, J. Biol. Chem. 278, 29072-29078.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29072-29078
    • Zickermann, V.1    Bostina, M.2    Hunte, C.3    Ruiz, T.4    Radermacher, M.5    Brandt, U.6
  • 38
    • 0034778053 scopus 로고    scopus 로고
    • Toward a characterization of the connecting module of complex I
    • Dupuis, A., Prieur, I., and Lunardi, J. (2001) Toward a characterization of the connecting module of complex I, J. Bioenerg. Biomembr. 33, 159-168.
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 159-168
    • Dupuis, A.1    Prieur, I.2    Lunardi, J.3
  • 39
    • 0035795163 scopus 로고    scopus 로고
    • Evidence for a quinone binding site close to the interface between NUOD and NUOB subunits of Complex I
    • Prieur, I., Lunardi, J., and Dupuis, A. (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
  • 40
    • 0034598939 scopus 로고    scopus 로고
    • A motif for quinone binding sites in respiratory and photosynthetic systems
    • Fisher, N., and Rich, P. R. (2000) A motif for quinone binding sites in respiratory and photosynthetic systems, J. Mol. Biol. 296, 1153-1162.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1153-1162
    • Fisher, N.1    Rich, P.R.2
  • 41
    • 0036321770 scopus 로고    scopus 로고
    • EPR characterization of ubisemiquinones and iron-sulfur cluster N2, central components of the energy coupling in the NADH-ubiquinone oxidoreductase (complex I) in situ
    • Magnitsky, S., Toulokhonova, L., Yano, T., Sled, V. D., Hagerhall, C., Grivennikova, V. G., Burbaev, D. S., Vinogradov, A. D., and Ohnishi, T. (2002) EPR characterization of ubisemiquinones and iron-sulfur cluster N2, central components of the energy coupling in the NADH-ubiquinone oxidoreductase (complex I) in situ, J. Bioenerg. Biomembr. 34, 193-208.
    • (2002) J. Bioenerg. Biomembr. , vol.34 , pp. 193-208
    • Magnitsky, S.1    Toulokhonova, L.2    Yano, T.3    Sled, V.D.4    Hagerhall, C.5    Grivennikova, V.G.6    Burbaev, D.S.7    Vinogradov, A.D.8    Ohnishi, T.9
  • 42
    • 0037815067 scopus 로고    scopus 로고
    • The ubiquinone-binding site in NADH: Ubiquinone oxidoreductase from Escherichia coli
    • Gong, X., Xie, T., Yu, L., Hesterberg, M., Scheide, D., Friedrich, T., and Yu, C. A. (2003) The ubiquinone-binding site in NADH: ubiquinone oxidoreductase from Escherichia coli, J. Biol. Chem. 278, 25731-25737.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25731-25737
    • Gong, X.1    Xie, T.2    Yu, L.3    Hesterberg, M.4    Scheide, D.5    Friedrich, T.6    Yu, C.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.