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Volumn 6, Issue 5, 2011, Pages 477-483

Decoupling of the catalytic and transport activities of complex i from Rhodothermus marinus by sodium/proton antiporter inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

5 (N ETHYL N ISOPROPYL)AMILORIDE; PROTON; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SODIUM ION;

EID: 79957477189     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb100380y     Document Type: Conference Paper
Times cited : (20)

References (31)
  • 1
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • DOI 10.1126/science.1123809
    • Sazanov, L. A. and Hinchliffe, P. (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus Science 311, 1430-1436 (Pubitemid 43376691)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 2
    • 77952979824 scopus 로고    scopus 로고
    • The architecture of respiratory complex i
    • Efremov, R. G., Baradaran, R., and Sazanov, L. A. (2010) The architecture of respiratory complex I Nature 465, 441-445
    • (2010) Nature , vol.465 , pp. 441-445
    • Efremov, R.G.1    Baradaran, R.2    Sazanov, L.A.3
  • 3
    • 77954848120 scopus 로고    scopus 로고
    • Functional modules and structural basis of conformational coupling in mitochondrial complex i
    • Hunte, C., Zickermann, V., and Brandt, U. (2010) Functional modules and structural basis of conformational coupling in mitochondrial complex I Science 329, 448-451
    • (2010) Science , vol.329 , pp. 448-451
    • Hunte, C.1    Zickermann, V.2    Brandt, U.3
  • 4
    • 0041563699 scopus 로고    scopus 로고
    • The 'antiporter module' of respiratory chain Complex I includes the MrpC/NuoK subunit - A revision of the modular evolution scheme
    • DOI 10.1016/S0014-5793(03)00767-1
    • Mathiesen, C. and Hagerhall, C. (2003) The "antiporter module" of respiratory chain complex I includes the MrpC/NuoK subunit- a revision of the modular evolution scheme FEBS Lett. 549, 7-13 (Pubitemid 36959834)
    • (2003) FEBS Letters , vol.549 , Issue.1-3 , pp. 7-13
    • Mathiesen, C.1    Hagerhall, C.2
  • 5
    • 0037010862 scopus 로고    scopus 로고
    • Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters
    • DOI 10.1016/S0005-2728(02)00343-2, PII S0005272802003432
    • Mathiesen, C. and Hagerhall, C. (2002) Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters Biochim. Biophys. Acta 1556, 121-132 (Pubitemid 35379670)
    • (2002) Biochimica et Biophysica Acta - Bioenergetics , vol.1556 , Issue.2-3 , pp. 121-132
    • Mathiesen, C.1    Hagerhall, C.2
  • 6
    • 0029910514 scopus 로고    scopus 로고
    • - stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells
    • Bogachev, A. V., Murtazina, R. A., and Skulachev, V. P. (1996) H+/e- stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells J. Bacteriol. 178, 6233-6237 (Pubitemid 26365704)
    • (1996) Journal of Bacteriology , vol.178 , Issue.21 , pp. 6233-6237
    • Bogachev, A.V.1    Murtazina, R.A.2    Skulachev, V.P.3
  • 7
    • 0032588194 scopus 로고    scopus 로고
    • +/2e stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles
    • DOI 10.1016/S0014-5793(99)00575-X, PII S001457939900575X
    • Galkin, A. S., Grivennikova, V. G., and Vinogradov, A. D. (1999) â†'H+/2e- stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles FEBS Lett. 451, 157-161 (Pubitemid 29231941)
    • (1999) FEBS Letters , vol.451 , Issue.2 , pp. 157-161
    • Galkin, A.S.1    Grivennikova, V.G.2    Vinogradov, A.D.3
  • 8
    • 0033955767 scopus 로고    scopus 로고
    • + translocation by complex I (NADH:quinone oxidoreductase) of Escherichia coli
    • DOI 10.1046/j.1365-2958.2000.01712.x
    • Steuber, J., Schmid, C., Rufibach, M., and Dimroth, P. (2000) Na+ translocation by complex I (NADH:quinone oxidoreductase) of Escherichia coli Mol. Microbiol. 35, 428-434 (Pubitemid 30055239)
    • (2000) Molecular Microbiology , vol.35 , Issue.2 , pp. 428-434
    • Steuber, J.1    Schmid, C.2    Rufibach, M.3    Dimroth, P.4
  • 9
    • 0037072803 scopus 로고    scopus 로고
    • The respiratory complex i (NDH I) from Klebsiella pneumoniae, a sodium pump
    • Gemperli, A. C., Dimroth, P., and Steuber, J. (2002) The respiratory complex I (NDH I) from Klebsiella pneumoniae, a sodium pump J. Biol. Chem. 277, 33811-33817
    • (2002) J. Biol. Chem. , vol.277 , pp. 33811-33817
    • Gemperli, A.C.1    Dimroth, P.2    Steuber, J.3
  • 11
    • 1842737600 scopus 로고    scopus 로고
    • The origin of the sodium-dependent NADH oxidation by the respiratory chain of Klebsiella pneumoniae
    • DOI 10.1016/S0014-5793(04)00312-6, PII S0014579304003126
    • Bertsova, Y. V. and Bogachev, A. V. (2004) The origin of the sodium-dependent NADH oxidation by the respiratory chain of Klebsiella pneumoniae FEBS Lett. 563, 207-212 (Pubitemid 38471600)
    • (2004) FEBS Letters , vol.563 , Issue.1-3 , pp. 207-212
    • Bertsova, Y.V.1    Bogachev, A.V.2
  • 12
    • 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
    • DOI 10.1074/jbc.M311242200
    • 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 (Pubitemid 38623253)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 18377-18383
    • Stolpe, S.1    Friedrich, T.2
  • 14
    • 0023807201 scopus 로고
    • Amiloride and its analogs as tools in the study of ion transport
    • Kleyman, T. R. and Cragoe, E. J., Jr. (1988) Amiloride and its analogs as tools in the study of ion transport J. Membr. Biol. 105, 1-21
    • (1988) J. Membr. Biol. , vol.105 , pp. 1-21
    • Kleyman, T.R.1    Cragoe Jr., E.J.2
  • 15
    • 0030696121 scopus 로고    scopus 로고
    • + antiporter from Vibrio parahaemolyticus
    • Kuroda, T., Shimamoto, T., Mizushima, T., and Tsuchiya, T. (1997) Mutational analysis of amiloride sensitivity of the NhaA Na+/H+ antiporter from Vibrio parahaemolyticus J. Bacteriol. 179, 7600-7602 (Pubitemid 27510004)
    • (1997) Journal of Bacteriology , vol.179 , Issue.23 , pp. 7600-7602
    • Kuroda, T.1    Shimamoto, T.2    Mizushima, T.3    Tsuchiya, T.4
  • 16
    • 0021840370 scopus 로고
    • + antiporter in Escherichia coli
    • Mochizuki-Oda, N. and Oosawa, F. (1985) Amiloride-sensitive Na+/H+ antiporter in Escherichia coli J. Bacteriol. 163, 395-397 (Pubitemid 15012767)
    • (1985) Journal of Bacteriology , vol.163 , Issue.1 , pp. 395-397
    • Mochizuki-Oda, N.1    Oosawa, F.2
  • 17
    • 0042064938 scopus 로고    scopus 로고
    • Amiloride inhibition of the proton-translocating NADH-quinone oxidoreductase of mammals and bacteria
    • DOI 10.1016/S0014-5793(03)00766-X
    • Nakamaru-Ogiso, E., Seo, B. B., Yagi, T., and Matsuno-Yagi, A. (2003) Amiloride inhibition of the proton-translocating NADH-quinone oxidoreductase of mammals and bacteria FEBS Lett. 549, 43-46 (Pubitemid 36959841)
    • (2003) FEBS Letters , vol.549 , Issue.1-3 , pp. 43-46
    • Nakamaru-Ogiso, E.1    Seo, B.B.2    Yagi, T.3    Matsuno-Yagi, A.4
  • 18
    • 0347295939 scopus 로고    scopus 로고
    • The ND5 subunit was labeled by a photoaffinity analogue of fenpyroximate in bovine mitochondrial complex I
    • DOI 10.1021/bi0269660
    • Nakamaru-Ogiso, E., Sakamoto, K., Matsuno-Yagi, A., Miyoshi, H., and Yagi, T. (2003) The ND5 subunit was labeled by a photoaffinity analogue of Fenpyroximate in bovine mitochondrial complex I Biochemistry 42, 746-754 (Pubitemid 36133299)
    • (2003) Biochemistry , vol.42 , Issue.3 , pp. 746-754
    • Nakamaru-Ogiso, E.1    Sakamoto, K.2    Matsuno-Yagi, A.3    Miyoshi, H.4    Yagi, T.5
  • 19
    • 0038712412 scopus 로고    scopus 로고
    • +
    • DOI 10.1074/jbc.M301682200
    • Steuber, J. (2003) The C-terminally truncated NuoL subunit (ND5 homologue) of the Na+-dependent complex I from Escherichia coli transports Na+ J. Biol. Chem. 278, 26817-26822 (Pubitemid 36876831)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 26817-26822
    • Steuber, J.1
  • 20
    • 47649115902 scopus 로고    scopus 로고
    • Mitochondrial Complex i superoxide production is attenuated by uncoupling
    • Dlaskova, A., Hlavata, L., Jezek, J., and Jezek, P. (2008) Mitochondrial Complex I superoxide production is attenuated by uncoupling Int. J. Biochem. Cell Biol. 40, 2098-2109
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 2098-2109
    • Dlaskova, A.1    Hlavata, L.2    Jezek, J.3    Jezek, P.4
  • 21
    • 0021769160 scopus 로고
    • Use of the pH sensitive fluorescence probe pyranine to monitor internal pH changes in Escherichia coli membrane vesicles
    • Damiano, E., Bassilana, M., Rigaud, J. L., and Leblanc, G. (1984) Use of the pH sensitive fluorescence probe pyranine to monitor internal pH changes in Escherichia coli membrane vesicles FEBS Lett. 166, 120-124
    • (1984) FEBS Lett. , vol.166 , pp. 120-124
    • Damiano, E.1    Bassilana, M.2    Rigaud, J.L.3    Leblanc, G.4
  • 22
    • 0026722859 scopus 로고
    • Assessment of uncoupling by amiloride analogs
    • Davies, K. and Solioz, M. (1992) Assessment of uncoupling by amiloride analogs Biochemistry 31, 8055-8058
    • (1992) Biochemistry , vol.31 , pp. 8055-8058
    • Davies, K.1    Solioz, M.2
  • 23
    • 0020794764 scopus 로고
    • A novel effect of amiloride on H+-dependent Na+ transport
    • Dubinsky, W. P., Jr. and Frizzell, R. A. (1983) A novel effect of amiloride on H+-dependent Na+ transport Am. J. Physiol. 245, C157-159
    • (1983) Am. J. Physiol. , vol.245 , pp. 157-159
    • Dubinsky Jr., W.P.1    Frizzell, R.A.2
  • 24
    • 70350351403 scopus 로고    scopus 로고
    • Structural basis for the mechanism of respiratory complex i
    • Berrisford, J. M. and Sazanov, L. A. (2009) Structural basis for the mechanism of respiratory complex I J. Biol. Chem. 284, 29773-29783
    • (2009) J. Biol. Chem. , vol.284 , pp. 29773-29783
    • Berrisford, J.M.1    Sazanov, L.A.2
  • 25
    • 0033604828 scopus 로고    scopus 로고
    • Membrane-bound electron transfer chain of the thermohalophilic bacterium Rhodothermus marinus: Characterization of the iron-sulfur centers from the dehydrogenases and investigation of the high-potential iron-sulfur protein function by in vitro reconstitution of the respiratory chain
    • Pereira, M. M., Carita, J. N., and Teixeira, M. (1999) Membrane-bound electron transfer chain of the thermohalophilic bacterium Rhodothermus marinus: characterization of the iron-sulfur centers from the dehydrogenases and investigation of the high-potential iron-sulfur protein function by in vitro reconstitution of the respiratory chain Biochemistry 38, 1276-1283
    • (1999) Biochemistry , vol.38 , pp. 1276-1283
    • Pereira, M.M.1    Carita, J.N.2    Teixeira, M.3
  • 26
    • 0018215206 scopus 로고
    • A one-step biuret assay for protein in the presence of detergent
    • Watters, C. (1978) A one-step biuret assay for protein in the presence of detergent Anal. Biochem. 88, 695-698 (Pubitemid 9112665)
    • (1978) Analytical Biochemistry , vol.88 , Issue.2 , pp. 695-698
    • Watters, C.1
  • 27
    • 31044432666 scopus 로고    scopus 로고
    • Electron paramagnetic resonance studies of the iron-sulfur centers from complex I of Rhodothermus marinus
    • DOI 10.1021/bi0519452
    • Fernandes, A. S., Sousa, F. L., Teixeira, M., and Pereira, M. M. (2006) Electron paramagnetic resonance studies of the iron-sulfur centers from complex I of Rhodothermus marinus Biochemistry 45, 1002-1008 (Pubitemid 43122264)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 1002-1008
    • Fernandes, A.S.1    Sousa, F.L.2    Teixeira, M.3    Pereira, M.M.4
  • 28
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • DOI 10.1016/0003-2697(85)90442-7
    • Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., and Klenk, D. C. (1985) Measurement of protein using bicinchoninic acid Anal. Biochem. 150, 76-85 (Pubitemid 16258399)
    • (1985) Analytical Biochemistry , vol.150 , Issue.1 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 29
    • 0023657856 scopus 로고
    • Oxonol VI as an optical indicator for membrane potentials in lipid vesicles
    • Apell, H. J. and Bersch, B. (1987) Oxonol VI as an optical indicator for membrane potentials in lipid vesicles Biochim. Biophys. Acta 903, 480-494
    • (1987) Biochim. Biophys. Acta , vol.903 , pp. 480-494
    • Apell, H.J.1    Bersch, B.2
  • 30
    • 0000193823 scopus 로고
    • +-ATPase from red beet (Beta vulgaris L.) storage tissue
    • Briskin, D. P. and Reynolds-Niesman, I. (1991) Determination of H/ATP Stoichiometry for the Plasma Membrane H-ATPase from Red Beet (Beta vulgaris L.) storage tissue Plant Physiol 95, 242-250 (Pubitemid 21913800)
    • (1991) Plant Physiology , vol.95 , Issue.1 , pp. 242-250
    • Briskin, D.P.1    Reynolds-Niesman, I.2
  • 31
    • 0037098935 scopus 로고    scopus 로고
    • 23Na NMR study of Fibrobacter succinogenes S85: Comparison of three chemical shift reagents and calculation of sodium concentration using ionophores
    • DOI 10.1006/abio.2002.5685
    • 23Na NMR study of Fibrobacter succinogenes S85: comparison of three chemical shift reagents and calculation of sodium concentration using ionophores Anal. Biochem. 306, 171-180 (Pubitemid 34791485)
    • (2002) Analytical Biochemistry , vol.306 , Issue.2 , pp. 171-180
    • Delort, A.-M.1    Gaudet, G.2    Forano, E.3


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