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Volumn 42, Issue 3, 2005, Pages 251-261

Direct transfer of NADH from malate dehydrogenase to complex I in Escherichia coli

Author keywords

Complex I; Direct transfer; Malate dehydrogenase; NADH:ubiquinone oxidoreductase; Proton translocation

Indexed keywords

MALATE DEHYDROGENASE; MULTIENZYME COMPLEX; NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 25844493709     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:42:3:251     Document Type: Article
Times cited : (12)

References (43)
  • 1
    • 0009672160 scopus 로고    scopus 로고
    • Special issue - Structure and function of complex I - Preface
    • Brandt, U. (1998) Special issue - structure and function of complex I - preface. Biochim. Biophys. Acta 1364, 85-86.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 85-86
    • Brandt, U.1
  • 2
    • 0023463947 scopus 로고
    • NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain
    • Matsushita, K., Ohnishi, T., and Kaback, H. R. (1987) NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry 26, 7732-7737.
    • (1987) Biochemistry , vol.26 , pp. 7732-7737
    • Matsushita, K.1    Ohnishi, T.2    Kaback, H.R.3
  • 3
    • 0027155827 scopus 로고
    • Energetic efficiency of Escherichia coli: Effects of mutations in components of the aerobic respiratory chain
    • Calhoun, M. W., Oden, K. L., Gennis, R. B., de Mattos, M. J., and Neijssel, O. M. (1993) Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain. J. Bacteriol. 175, 3020-3025.
    • (1993) J. Bacteriol. , vol.175 , pp. 3020-3025
    • Calhoun, M.W.1    Oden, K.L.2    Gennis, R.B.3    De Mattos, M.J.4    Neijssel, O.M.5
  • 4
    • 0035342619 scopus 로고    scopus 로고
    • Na(+) translocation by bacterial NADH:quinone oxidoreductases: An extension to the complex-I family of primary redox pumps
    • Steuber, J. (2001) Na(+) translocation by bacterial NADH:quinone oxidoreductases: an extension to the complex-I family of primary redox pumps. Biochim. Biophys. Acta 1505, 45-56.
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 45-56
    • Steuber, J.1
  • 5
    • 0022515187 scopus 로고
    • Organization of citric acid cycle enzymes into a multienzyme cluster
    • Barnes, S. J. and Weitzman, P. D. (1986) Organization of citric acid cycle enzymes into a multienzyme cluster. FEBS Lett. 201, 267-270.
    • (1986) FEBS Lett. , vol.201 , pp. 267-270
    • Barnes, S.J.1    Weitzman, P.D.2
  • 6
    • 0023644515 scopus 로고
    • Further characterization of the Krebs tricarboxylic acid cycle metabolon
    • Robinson, J. B., Jr., Inman, L., Sumegi, B., and Srere, P. A. (1987) Further characterization of the Krebs tricarboxylic acid cycle metabolon. J. Biol. Chem. 262, 1786-1790.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1786-1790
    • Robinson Jr., J.B.1    Inman, L.2    Sumegi, B.3    Srere, P.A.4
  • 7
    • 0040777075 scopus 로고    scopus 로고
    • Model of a quinary structure between Krebs TCA cycle enzymes: A model for the metabolon
    • Velot, C., Mixon, M. B., Teige, M., and Srere, P. A. (1997) Model of a quinary structure between Krebs TCA cycle enzymes: a model for the metabolon. Biochemistry 36, 14271-14276.
    • (1997) Biochemistry , vol.36 , pp. 14271-14276
    • Velot, C.1    Mixon, M.B.2    Teige, M.3    Srere, P.A.4
  • 8
    • 0021744544 scopus 로고
    • Complex I binds several mitochondrial NAD-coupled dehydrogenases
    • Sumegi, B. and Srere, P. A. (1984) Complex I binds several mitochondrial NAD-coupled dehydrogenases. J. Biol. Chem. 259, 15040-15045.
    • (1984) J. Biol. Chem. , vol.259 , pp. 15040-15045
    • Sumegi, B.1    Srere, P.A.2
  • 9
    • 0022816351 scopus 로고
    • Metabolite transfer via enzyme-enzyme complexes
    • Srivastava, D. K. and Bernhard, S. A. (1986) Metabolite transfer via enzyme-enzyme complexes. Science 234, 1081-1086.
    • (1986) Science , vol.234 , pp. 1081-1086
    • Srivastava, D.K.1    Bernhard, S.A.2
  • 10
    • 0343638632 scopus 로고
    • The combination of diphosphopyridine nucleotide with glyceraldehyde phosphate dehydrogenase
    • Cori, C. F., Velick, S. F., and Cori, G. T. (1950) The combination of diphosphopyridine nucleotide with glyceraldehyde phosphate dehydrogenase. Biochim. Biophys. Acta 4, 160-169.
    • (1950) Biochim. Biophys. Acta , vol.4 , pp. 160-169
    • Cori, C.F.1    Velick, S.F.2    Cori, G.T.3
  • 11
    • 25744449268 scopus 로고
    • Interaction between glyceraldehyde phosphate dehydrogenase and DPNH-cytochrome reductase
    • Mahler, H. R. and Elowe, D. (1954) Interaction between glyceraldehyde phosphate dehydrogenase and DPNH-cytochrome reductase. Biochim. Biophys. Acta 14, 100-107.
    • (1954) Biochim. Biophys. Acta , vol.14 , pp. 100-107
    • Mahler, H.R.1    Elowe, D.2
  • 12
    • 25844448683 scopus 로고
    • Interaction of pyridine-nucleotide linked enzymes
    • Nygaard, A. P. and Rutter, W. J. (1956) Interaction of pyridine-nucleotide linked enzymes. Acta Chem. Scand. 10, 37-48.
    • (1956) Acta Chem. Scand. , vol.10 , pp. 37-48
    • Nygaard, A.P.1    Rutter, W.J.2
  • 13
    • 0015326559 scopus 로고
    • The stereospecificity of nicotinamide-adenine dinucleotide-dependent oxidoreductases from plants
    • Davies, D. D., Teixeira, A., and Kenworthy, P. (1972) The stereospecificity of nicotinamide-adenine dinucleotide-dependent oxidoreductases from plants. Biochem. J. 127, 335-343.
    • (1972) Biochem. J. , vol.127 , pp. 335-343
    • Davies, D.D.1    Teixeira, A.2    Kenworthy, P.3
  • 14
    • 0028674909 scopus 로고
    • Binding of malate dehydrogenase and NADH channelling to complex I
    • Ovadi, J., Huang, Y., and Spivey, H. O. (1994) Binding of malate dehydrogenase and NADH channelling to complex I. J. Mol. Recognit. 7, 265-272.
    • (1994) J. Mol. Recognit. , vol.7 , pp. 265-272
    • Ovadi, J.1    Huang, Y.2    Spivey, H.O.3
  • 15
    • 0024468918 scopus 로고
    • Substrate channeling of NADH and binding of dehydrogenases to complex I
    • Fukushima, T., Decker, R. V., Anderson, W. M., and Spivey, H. O. (1989) Substrate channeling of NADH and binding of dehydrogenases to complex I. J. Biol. Chem. 264, 16483-16488.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16483-16488
    • Fukushima, T.1    Decker, R.V.2    Anderson, W.M.3    Spivey, H.O.4
  • 16
    • 0013855171 scopus 로고
    • Stereospecificity of certain soluble and particulate preparations of mitochondrial reduced nicotinamide-adenine dinucleotide dehydrogenase from beef heart
    • Ernster, L., Hoberman, H. D., Howard, R. L., King, T. E., Lee, C. P., Mackler, B., et al. (1965) Stereospecificity of certain soluble and particulate preparations of mitochondrial reduced nicotinamide-adenine dinucleotide dehydrogenase from beef heart. Nature 207, 940-941.
    • (1965) Nature , vol.207 , pp. 940-941
    • Ernster, L.1    Hoberman, H.D.2    Howard, R.L.3    King, T.E.4    Lee, C.P.5    Mackler, B.6
  • 17
    • 2442599389 scopus 로고    scopus 로고
    • Absence of NADH channeling in coupled reaction of mitochondrial malate dehydrogenase and complex I in alamethicin-permeabilized rat liver mitochondria
    • Kotlyar, A. B., Maklashina, E., and Cecchini, G. (2004) Absence of NADH channeling in coupled reaction of mitochondrial malate dehydrogenase and complex I in alamethicin-permeabilized rat liver mitochondria. Biochem. Biophys. Res. Commun. 318, 987-991.
    • (2004) Biochem. Biophys. Res. Commun. , vol.318 , pp. 987-991
    • Kotlyar, A.B.1    Maklashina, E.2    Cecchini, G.3
  • 18
    • 0023061429 scopus 로고
    • Complexes of sequential metabolic enzymes
    • Srere, P. A. (1987) Complexes of sequential metabolic enzymes. Annu. Rev. Biochem. 56, 89-124.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 89-124
    • Srere, P.A.1
  • 19
    • 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
  • 20
    • 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., and Weiss, H. (1993) 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. 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
  • 21
    • 0030070202 scopus 로고    scopus 로고
    • Comparison of the inhibitory action of synthetic capsaicin analogues with various NADH-ubiquinone oxidoreductases
    • Satoh, T., Miyoshi, H., Sakamoto, K., and Iwamura, H. (1996) Comparison of the inhibitory action of synthetic capsaicin analogues with various NADH-ubiquinone oxidoreductases. Biochim. Biophys. Acta 1273, 21-30.
    • (1996) Biochim. Biophys. Acta , vol.1273 , pp. 21-30
    • Satoh, T.1    Miyoshi, H.2    Sakamoto, K.3    Iwamura, H.4
  • 22
    • 0025886175 scopus 로고
    • Purification and crystallization of recombinant Escherichia coli malate dehydrogenase
    • Hall, M. D., Levitt, D. G., McAlister-Henn, L., and Banaszak, L. J. (1991) Purification and crystallization of recombinant Escherichia coli malate dehydrogenase. J. Mol. Biol. 220, 551-553.
    • (1991) J. Mol. Biol. , vol.220 , pp. 551-553
    • Hall, M.D.1    Levitt, D.G.2    McAlister-Henn, L.3    Banaszak, L.J.4
  • 23
    • 0037995650 scopus 로고    scopus 로고
    • Mutagenesis of subunit N of the Escherichia coli Complex I. Identification of the initiation codon and the sensitivity of mutants to decylubiquinone
    • Amarneh, B. and Vik, S. B. (2003) Mutagenesis of subunit N of the Escherichia coli Complex I. Identification of the initiation codon and the sensitivity of mutants to decylubiquinone. Biochemistry 42, 4800-1808.
    • (2003) Biochemistry , vol.42 , pp. 4800-11808
    • Amarneh, B.1    Vik, S.B.2
  • 24
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 26
    • 0029910514 scopus 로고    scopus 로고
    • - stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells
    • - stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells. J. Bacteriol. 178, 6233-6237.
    • (1996) J. Bacteriol. , vol.178 , pp. 6233-6237
    • Bogachev, A.V.1    Murtazina, R.A.2    Skulachev, V.P.3
  • 27
    • 2442473296 scopus 로고    scopus 로고
    • The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton-pump but may be capable of secondary sodium antiport
    • Stolpe, S. and Friedrich, T. (2004) The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton-pump but may be capable of secondary sodium antiport. J. Biol. Chem. 279, 18377-18383.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18377-18383
    • Stolpe, S.1    Friedrich, T.2
  • 29
    • 0025007820 scopus 로고
    • Inhibition by capsaicin of NADH-quinone oxidoreductases is correlated with the presence of energy-coupling site 1 in various organisms
    • Yagi, T. (1990) Inhibition by capsaicin of NADH-quinone oxidoreductases is correlated with the presence of energy-coupling site 1 in various organisms. Arch. Biochem. Biophys. 281, 305-311.
    • (1990) Arch. Biochem. Biophys. , vol.281 , pp. 305-311
    • Yagi, T.1
  • 30
    • 0028815572 scopus 로고
    • Regulation of malate dehydrogenase (mdh) gene expression in Escherichia coli in response to oxygen, carbon, and heme availability
    • Park, S. J., Cotter, P. A., and Gunsalus, R. P. (1995) Regulation of malate dehydrogenase (mdh) gene expression in Escherichia coli in response to oxygen, carbon, and heme availability. J. Bacteriol. 177, 6652-6656.
    • (1995) J. Bacteriol. , vol.177 , pp. 6652-6656
    • Park, S.J.1    Cotter, P.A.2    Gunsalus, R.P.3
  • 31
    • 0027175822 scopus 로고
    • Demonstration of separate genetic loci encoding distinct membrane-bound respiratory NADH dehydrogenases in Escherichia coli
    • Calhoun, M. W. and Gennis, R. B. (1993) Demonstration of separate genetic loci encoding distinct membrane-bound respiratory NADH dehydrogenases in Escherichia coli. J. Bacteriol. 175, 3013-3019.
    • (1993) J. Bacteriol. , vol.175 , pp. 3013-3019
    • Calhoun, M.W.1    Gennis, R.B.2
  • 32
    • 0033594863 scopus 로고    scopus 로고
    • A novel, definitive test for substrate channeling illustrated with the aspartate aminotransferase/malate dehydrogenase system
    • Geck, M. K. and Kirsch, J. F. (1999) A novel, definitive test for substrate channeling illustrated with the aspartate aminotransferase/malate dehydrogenase system. Biochemistry 38, 8032-8037.
    • (1999) Biochemistry , vol.38 , pp. 8032-8037
    • Geck, M.K.1    Kirsch, J.F.2
  • 34
    • 0027302991 scopus 로고
    • Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 A resolution
    • Hall, M. D., and Banaszak, L. J. (1993) Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 A resolution. J. Mol. Biol. 232, 213-222.
    • (1993) J. Mol. Biol. , vol.232 , pp. 213-222
    • Hall, M.D.1    Banaszak, L.J.2
  • 35
    • 0029075136 scopus 로고
    • Isolation and characterization of the proton-translocating NADH: Ubiquinone oxidoreductase from Escherichia coli
    • Leif, H., Sled, V. D., Ohnishi, T., Weiss, H., and Friedrich, T. (1995) Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem. 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
  • 36
    • 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
  • 38
    • 0014528704 scopus 로고
    • Catalytic mechanism of pig heart mitochondrial malate dehydrogenase studied by kinetics at equilibrium
    • Silverstein, E. and Sulebele, G. (1969) Catalytic mechanism of pig heart mitochondrial malate dehydrogenase studied by kinetics at equilibrium. Biochemistry 8, 2543-2550.
    • (1969) Biochemistry , vol.8 , pp. 2543-2550
    • Silverstein, E.1    Sulebele, G.2
  • 39
    • 0034462324 scopus 로고    scopus 로고
    • Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Escherichia coli
    • van der Rest, M. E., Frank, C., and Molenaar, D. (2000) Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Escherichia coli. J. Bacteriol. 182, 6892-6899.
    • (2000) J. Bacteriol. , vol.182 , pp. 6892-6899
    • Van Der Rest, M.E.1    Frank, C.2    Molenaar, D.3
  • 40
    • 0023109230 scopus 로고
    • Mechanism of transfer of reduced nicotinamide adenine dinucleotide among dehydrogenases. Transfer rates and equilibria with enzyme-enzyme complexes
    • Srivastava, D. K. and Bernhard, S. A. (1987) Mechanism of transfer of reduced nicotinamide adenine dinucleotide among dehydrogenases. Transfer rates and equilibria with enzyme-enzyme complexes. Biochemistry 26, 1240-1246.
    • (1987) Biochemistry , vol.26 , pp. 1240-1246
    • Srivastava, D.K.1    Bernhard, S.A.2
  • 41
    • 0021770898 scopus 로고
    • Direct transfer of reduced nicotinamide adenine dinucleotide from glyceraldehyde-3-phosphate dehydrogenase to liver alcohol dehydrogenase
    • Srivastava, D. K. and Bernhard, S. A. (1984) Direct transfer of reduced nicotinamide adenine dinucleotide from glyceraldehyde-3-phosphate dehydrogenase to liver alcohol dehydrogenase. Biochemistry 23, 4538-4545.
    • (1984) Biochemistry , vol.23 , pp. 4538-4545
    • Srivastava, D.K.1    Bernhard, S.A.2
  • 42
    • 0024385271 scopus 로고
    • Direct transfer of NADH between α-glycerol phosphate dehydrogenase and lactate dehydrogenase: Fact or misinterpretation?
    • Srivastava, D. K., Smolen, P., Betts, G. F., Fukushima, T., Spivey, H. O., and Bernhard, S. A. (1989) Direct transfer of NADH between α-glycerol phosphate dehydrogenase and lactate dehydrogenase: fact or misinterpretation? Proc. Natl. Acad. Sci. USA 86, 6464-6468.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6464-6468
    • Srivastava, D.K.1    Smolen, P.2    Betts, G.F.3    Fukushima, T.4    Spivey, H.O.5    Bernhard, S.A.6
  • 43
    • 0033534162 scopus 로고    scopus 로고
    • Overexpression of the Escherichia coli nuo-operon and isolation of the overproduced NADH:ubiquinone oxidoreductase (complex I)
    • Spehr, V., Schlitt, A., Scheide, D., Guénebaut, V., and Friedrich, T. (1999) Overexpression of the Escherichia coli nuo-operon and isolation of the overproduced NADH:ubiquinone oxidoreductase (complex I). Biochemistry 38, 16261-16267.
    • (1999) Biochemistry , vol.38 , pp. 16261-16267
    • Spehr, V.1    Schlitt, A.2    Scheide, D.3    Guénebaut, V.4    Friedrich, T.5


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