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Volumn 1710, Issue 2-3, 2005, Pages 87-95

Proton pumping by complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica reconstituted into proteoliposomes

Author keywords

Complex I; H+ pumping; Mitochondria; Reconstitution; Yarrowia lipolytica

Indexed keywords

AZOLECTIN; DETERGENT; DYE; GLUCOPYRANOSIDE; IONOPHORE; LIPOSOME; OCTYL BETA GLUCOSIDE; PHOSPHOLIPID; PROTON PUMP; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SODIUM ION; UNCLASSIFIED DRUG;

EID: 28244435454     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2005.10.001     Document Type: Article
Times cited : (41)

References (42)
  • 1
    • 0038392255 scopus 로고    scopus 로고
    • Proton pumping by NADH:ubiquinone oxidoreductase. a redox driven conformational change mechanism?
    • U. Brandt, S. Kerscher, S. Dröse, K. Zwicker, and V. Zickermann Proton pumping by NADH:ubiquinone oxidoreductase. A redox driven conformational change mechanism? FEBS Lett. 545 2003 9 17
    • (2003) FEBS Lett. , vol.545 , pp. 9-17
    • Brandt, U.1    Kerscher, S.2    Dröse, S.3    Zwicker, K.4    Zickermann, V.5
  • 4
    • 0031033436 scopus 로고    scopus 로고
    • Proton-translocation by membrane-bound NADH:Ubiquinone-oxidoreductase (complex I) through redox-gated ligand conduction
    • U. Brandt Proton-translocation by membrane-bound NADH:Ubiquinone- oxidoreductase (complex I) through redox-gated ligand conduction Biochim. Biophys. Acta 1318 1997 79 91
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 79-91
    • Brandt, U.1
  • 5
    • 0033000256 scopus 로고    scopus 로고
    • Proton translocation in the respiratory chain involving ubiquinone-A hypothetical semiquinone switch mechanism for complex I
    • U. Brandt Proton translocation in the respiratory chain involving ubiquinone-A hypothetical semiquinone switch mechanism for complex I BioFactors 9 1999 95 101
    • (1999) BioFactors , vol.9 , pp. 95-101
    • Brandt, U.1
  • 6
  • 7
    • 0032852758 scopus 로고    scopus 로고
    • EPR studies of the possible binding sites of the cluster N2, semiquinones, and specific inhibitors of the NADH:quinone oxidoreductase (complex I)
    • T. Ohnishi, S. Magnitsky, L. Toulokhonova, T. Yano, T. Yagi, D.S. Burbaev, and A.D. Vinogradov EPR studies of the possible binding sites of the cluster N2, semiquinones, and specific inhibitors of the NADH:quinone oxidoreductase (complex I) Biochem. Soc. Trans. 27 1999 586 591
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 586-591
    • Ohnishi, T.1    Magnitsky, S.2    Toulokhonova, L.3    Yano, T.4    Yagi, T.5    Burbaev, D.S.6    Vinogradov, A.D.7
  • 9
    • 0028277764 scopus 로고
    • The protonmotive Q cycle in mitochondria and bacteria
    • U. Brandt, and B.L. Trumpower The protonmotive Q cycle in mitochondria and bacteria CRC Crit. Rev. Biochem. 29 1994 165 197
    • (1994) CRC Crit. Rev. Biochem. , vol.29 , pp. 165-197
    • Brandt, U.1    Trumpower, B.L.2
  • 10
    • 0043208847 scopus 로고    scopus 로고
    • Functional implications from an unexpected position of the 49 kDa subunit of complex I
    • V. Zickermann, M. Bostina, C. Hunte, T. Ruiz, M. Radermacher, and U. Brandt Functional implications from an unexpected position of the 49 kDa subunit of complex I J. Biol. Chem. 278 2003 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
  • 11
    • 2542421934 scopus 로고    scopus 로고
    • Substrate-induced conformational change in bacterial complex I
    • A.A. Mamedova, P.J. Holt, J. Carroll, and L.A. Sazanov Substrate-induced conformational change in bacterial complex I J. Biol. Chem. 279 2004 23830 23836
    • (2004) J. Biol. Chem. , vol.279 , pp. 23830-23836
    • Mamedova, A.A.1    Holt, P.J.2    Carroll, J.3    Sazanov, L.A.4
  • 12
    • 2442484666 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic study on the conformational reorganization in Escherichia coli complex I due to redox-driven proton translocation
    • P. Hellwig, S. Stolpe, and T. Friedrich Fourier transform infrared spectroscopic study on the conformational reorganization in Escherichia coli complex I due to redox-driven proton translocation Biopolymers 74 2004 69 72
    • (2004) Biopolymers , vol.74 , pp. 69-72
    • Hellwig, P.1    Stolpe, S.2    Friedrich, T.3
  • 13
    • 0032478597 scopus 로고    scopus 로고
    • Mitochondrial NADH-ubiquinone oxidoreductase (complex I). Effect of substrates on the fragmentation of subunits by trypsin
    • M. Yamaguchi, G. Belogrudov, and Y. Hatefi Mitochondrial NADH-ubiquinone oxidoreductase (complex I). Effect of substrates on the fragmentation of subunits by trypsin J. Biol. Chem. 273 1998 8094 8098
    • (1998) J. Biol. Chem. , vol.273 , pp. 8094-8098
    • Yamaguchi, M.1    Belogrudov, G.2    Hatefi, Y.3
  • 14
    • 0021769852 scopus 로고
    • Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone
    • M.K.F. Wikström Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone FEBS Lett. 169 1984 300 304
    • (1984) FEBS Lett. , vol.169 , pp. 300-304
    • Wikström, M.K.F.1
  • 15
    • 0035297567 scopus 로고    scopus 로고
    • - stoichiometry of the NADH:ubiquinone reductase reaction catalyzed by submitochondrial particles
    • - stoichiometry of the NADH:ubiquinone reductase reaction catalyzed by submitochondrial particles Biochemistry (Mosc.) 66 2001 435 443
    • (2001) Biochemistry (Mosc.) , vol.66 , pp. 435-443
    • Galkin, A.S.1    Grivennikova, V.G.2    Vinogradov, A.D.3
  • 16
    • 0017113635 scopus 로고
    • Electron transport in aerobically grown Paracoccus denitrificans: Kinetic characterization of the membrane-bound cytochromes and the stoichiometry of respiration-driven proton translocation
    • H.G. Lawford, J.C. Cox, P.B. Garland, and B.A. Haddock Electron transport in aerobically grown Paracoccus denitrificans: kinetic characterization of the membrane-bound cytochromes and the stoichiometry of respiration-driven proton translocation FEBS Lett. 64 1976 369 374
    • (1976) FEBS Lett. , vol.64 , pp. 369-374
    • Lawford, H.G.1    Cox, J.C.2    Garland, P.B.3    Haddock, B.A.4
  • 17
    • 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 1996 6233 6237
    • (1996) J. Bacteriol. , vol.178 , pp. 6233-6237
    • Bogachev, A.V.1    Murtazina, R.A.2    Skulachev, V.P.3
  • 18
    • 0015841465 scopus 로고
    • Energy transduction in photosynthetic bacteria: VI. Respiratory sites of energy conservation in membranes from dark-grown cells of Rhodopseudomonas capsulata
    • A. Baccarini Melandri, D. Zannoni, and B.A. Melandri Energy transduction in photosynthetic bacteria: VI. Respiratory sites of energy conservation in membranes from dark-grown cells of Rhodopseudomonas capsulata Biochim. Biophys. Acta 314 1973 298 311
    • (1973) Biochim. Biophys. Acta , vol.314 , pp. 298-311
    • Baccarini Melandri, A.1    Zannoni, D.2    Melandri, B.A.3
  • 19
    • 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
    • S. Stolpe, and T. Friedrich 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 2004 18377 18383
    • (2004) J. Biol. Chem. , vol.279 , pp. 18377-18383
    • Stolpe, S.1    Friedrich, T.2
  • 20
    • 0037417865 scopus 로고    scopus 로고
    • Sodium ion cycling mediates energy coupling between complex I and ATP synthase
    • A.C. Gemperli, P. Dimroth, and J. Steuber Sodium ion cycling mediates energy coupling between complex I and ATP synthase Proc. Natl. Acad. Sci. U. S. A. 100 2003 839 844
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 839-844
    • Gemperli, A.C.1    Dimroth, P.2    Steuber, J.3
  • 21
    • 0037072803 scopus 로고    scopus 로고
    • The respiratory complex I (NDH I) from Klebsiella pneumoniae, a sodium pump
    • A.C. Gemperli, P. Dimroth, and J. Steuber The respiratory complex I (NDH I) from Klebsiella pneumoniae, a sodium pump J. Biol. Chem. 277 2002 33811 33817
    • (2002) J. Biol. Chem. , vol.277 , pp. 33811-33817
    • Gemperli, A.C.1    Dimroth, P.2    Steuber, J.3
  • 22
    • 1842737600 scopus 로고    scopus 로고
    • The origin of the sodium-dependent NADH oxidation by the respiratory chain of Klebsiella pneumoniae
    • Y.V. Bertsova, and A.V. Bogachev The origin of the sodium-dependent NADH oxidation by the respiratory chain of Klebsiella pneumoniae FEBS Lett. 563 2004 207 212
    • (2004) FEBS Lett. , vol.563 , pp. 207-212
    • Bertsova, Y.V.1    Bogachev, A.V.2
  • 23
    • 0034604568 scopus 로고    scopus 로고
    • Function of conserved acidic residues in the PSST-homologue of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica
    • P. Ahlers, K. Zwicker, S. Kerscher, and U. Brandt Function of conserved acidic residues in the PSST-homologue of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica J. Biol. Chem. 275 2000 23577 23582
    • (2000) J. Biol. Chem. , vol.275 , pp. 23577-23582
    • Ahlers, P.1    Zwicker, K.2    Kerscher, S.3    Brandt, U.4
  • 24
    • 0035968167 scopus 로고    scopus 로고
    • A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I
    • N. Kashani-Poor, K. Zwicker, S. Kerscher, and U. Brandt A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I J. Biol. Chem. 276 2001 24082 24087
    • (2001) J. Biol. Chem. , vol.276 , pp. 24082-24087
    • Kashani-Poor, N.1    Zwicker, K.2    Kerscher, S.3    Brandt, U.4
  • 25
    • 0142149098 scopus 로고    scopus 로고
    • Two aspartic acid residues in the PSST-homologous NUKM subunit of complex I from Yarrowia lipolytica are essential for catalytic activity
    • A. Garofano, K. Zwicker, S. Kerscher, P. Okun, and U. Brandt Two aspartic acid residues in the PSST-homologous NUKM subunit of complex I from Yarrowia lipolytica are essential for catalytic activity J. Biol. Chem. 278 2003 42435 42440
    • (2003) J. Biol. Chem. , vol.278 , pp. 42435-42440
    • Garofano, A.1    Zwicker, K.2    Kerscher, S.3    Okun, P.4    Brandt, U.5
  • 26
    • 2442701768 scopus 로고    scopus 로고
    • Functional significance of conserved histidines and arginines in the 49 kDa subunit of mitochondrial complex I
    • L. Grgic, K. Zwicker, N. Kashani-Poor, S. Kerscher, and U. Brandt Functional significance of conserved histidines and arginines in the 49 kDa subunit of mitochondrial complex I J. Biol. Chem. 279 2004 21193 21199
    • (2004) J. Biol. Chem. , vol.279 , pp. 21193-21199
    • Grgic, L.1    Zwicker, K.2    Kashani-Poor, N.3    Kerscher, S.4    Brandt, U.5
  • 27
    • 0037015686 scopus 로고    scopus 로고
    • Full recovery of the NADH:ubiquinone activity of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica by the addition of phospholipids
    • S. Dröse, K. Zwicker, and U. Brandt Full recovery of the NADH:ubiquinone activity of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica by the addition of phospholipids Biochim. Biophys. Acta-Bioenerg. 1556 2002 65 72
    • (2002) Biochim. Biophys. Acta-Bioenerg. , vol.1556 , pp. 65-72
    • Dröse, S.1    Zwicker, K.2    Brandt, U.3
  • 28
    • 0035795187 scopus 로고    scopus 로고
    • Efficient large scale purification of his-tagged proton translocating NADH:ubiquinone oxidoreductase (complex I) from the strictly aerobic yeast Yarrowia lipolytica
    • N. Kashani-Poor, S. Kerscher, V. Zickermann, and U. Brandt Efficient large scale purification of his-tagged proton translocating NADH:ubiquinone oxidoreductase (complex I) from the strictly aerobic yeast Yarrowia lipolytica Biochim. Biophys. Acta 1504 2001 363 370
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 363-370
    • Kashani-Poor, N.1    Kerscher, S.2    Zickermann, V.3    Brandt, U.4
  • 31
    • 0032812743 scopus 로고    scopus 로고
    • A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica
    • S. Kerscher, J.G. Okun, and U. Brandt A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica J. Cell Sci. 112 1999 2347 2354
    • (1999) J. Cell Sci. , vol.112 , pp. 2347-2354
    • Kerscher, S.1    Okun, J.G.2    Brandt, U.3
  • 32
    • 0029101114 scopus 로고
    • Reconstitution of membrane proteins into liposomes: Application to energy-transducing membrane proteins
    • J.-L. Rigaud, B. Pitard, and R.M. Levy Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins Biochim. Biophys. Acta 1231 1995 223 246
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 223-246
    • Rigaud, J.-L.1    Pitard, B.2    Levy, R.M.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, and U. Brandt Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica Biochim. Biophys. Acta 1459 2000 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
    • 0032829920 scopus 로고    scopus 로고
    • Properties of the common inhibitor binding domain in mitochondrial NADH-dehydrogenase (complex I)
    • J.G. Okun, V. Zickermann, and U. Brandt Properties of the common inhibitor binding domain in mitochondrial NADH-dehydrogenase (complex I) Biochem. Soc. Trans. 27 1999 596 601
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 596-601
    • Okun, J.G.1    Zickermann, V.2    Brandt, U.3
  • 36
    • 0034691659 scopus 로고    scopus 로고
    • Binding of detergents and inhibitors to bovine complex I-A novel purification procedure of bovine complex I retaining full inhibitor sensitivity
    • J.G. Okun, V. Zickermann, K. Zwicker, H. Schägger, and U. Brandt Binding of detergents and inhibitors to bovine complex I-A novel purification procedure of bovine complex I retaining full inhibitor sensitivity Biochim. Biophys. Acta-Bioenerg. 1459 2000 77 87
    • (2000) Biochim. Biophys. Acta-Bioenerg. , vol.1459 , pp. 77-87
    • Okun, J.G.1    Zickermann, V.2    Zwicker, K.3    Schägger, H.4    Brandt, U.5
  • 37
    • 0020661801 scopus 로고
    • Mechanistic differences in the energy-linked fluorescence decreases of 9-aminoacridine dyes associated with bovine heart submitochondrial membranes
    • C.S. Huang, J. Kopecky, and C.P. Lee Mechanistic differences in the energy-linked fluorescence decreases of 9-aminoacridine dyes associated with bovine heart submitochondrial membranes Biochim. Biophys. Acta 722 1983 107 115
    • (1983) Biochim. Biophys. Acta , vol.722 , pp. 107-115
    • Huang, C.S.1    Kopecky, J.2    Lee, C.P.3
  • 38
    • 0017650832 scopus 로고
    • Thermodynamics of the electrochemical proton gradient in bovine heart submitochondrial particles
    • C.L. Bashford, and W.S. Thayer Thermodynamics of the electrochemical proton gradient in bovine heart submitochondrial particles J. Biol. Chem. 252 1977 8459 8463
    • (1977) J. Biol. Chem. , vol.252 , pp. 8459-8463
    • Bashford, C.L.1    Thayer, W.S.2
  • 39
    • 0016766648 scopus 로고
    • Ion transport and respiratory control in vesicles formed from reduced nicotinamid adenine dinucleotide coenzyme Q reductase and phospholipids
    • C.I. Ragan, and P.C. Hinkle Ion transport and respiratory control in vesicles formed from reduced nicotinamid adenine dinucleotide coenzyme Q reductase and phospholipids J. Biol. Chem. 250 1975 8472 8476
    • (1975) J. Biol. Chem. , vol.250 , pp. 8472-8476
    • Ragan, C.I.1    Hinkle, P.C.2
  • 41
    • 0034783532 scopus 로고    scopus 로고
    • +-translocating NADH:quinone oxidoreductase (NDH I) from Klebsiella pneumoniae and Escherichia coli: Implications for the mechanism of redox-driven cation translocation by complex I
    • +-translocating NADH:quinone oxidoreductase (NDH I) from Klebsiella pneumoniae and Escherichia coli: implications for the mechanism of redox-driven cation translocation by complex I J. Bioenerg. Biomembr. 33 2001 186 197
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 186-197
    • Steuber, J.1
  • 42
    • 0032781876 scopus 로고    scopus 로고
    • + translocation by theNADH:ubiquinone oxidoreductase (complex I) from Klebsiella pneumoniae
    • + translocation by theNADH:ubiquinone oxidoreductase (complex I) from Klebsiella pneumoniae Mol. Microbiol. 33 1999 590 598
    • (1999) Mol. Microbiol. , vol.33 , pp. 590-598
    • Krebs, W.1    Steuber, J.2    Gemperli, A.C.3    Dimroth, P.4


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