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Volumn 48, Issue 40, 2009, Pages 9516-9524

Acid residues in the transmembrane helices of the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae involved in sodium translocation

Author keywords

[No Author keywords available]

Indexed keywords

ACID RESIDUES; ASPARTATES; HYDROPHOBIC CORE; NEGATIVE CHARGE; OXIDOREDUCTASES; PATHOGENIC BACTERIUM; QUINONE REDUCTASE; RESPIRATORY COMPLEX; SODIUM IONS; TRANSLOCATION PROCESS; TRANSMEMBRANE HELICES; UBIQUINONE; VIBRIO CHOLERAE;

EID: 70350043311     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900845y     Document Type: Article
Times cited : (50)

References (31)
  • 1
    • 0021985263 scopus 로고
    • +-motive NADH oxidase in inverted membrane vesicles of Vibrio alginolyticus
    • +-motive NADH oxidase in inverted membrane vesicles of Vibrio alginolyticus. FEBS Lett. 183, 95-98.
    • (1985) FEBS Lett , vol.183 , pp. 95-98
    • Tokuda, H.1    Udagawa, T.2    Unemoto, T.3
  • 2
    • 0035342631 scopus 로고    scopus 로고
    • +-translocating NADH-quinone reductase from the marine Vibrio alginolyticus
    • +-translocating NADH-quinone reductase from the marine Vibrio alginolyticus. Biochim. Biophys. Acta 1505, 37-44.
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 37-44
    • Hayashi, M.1    Nakayama, Y.2    Unemoto, T.3
  • 3
    • 17144423915 scopus 로고    scopus 로고
    • +-translocating NADH: Quinone oxidoreductase: Progress achieved and prospects of investigations
    • DOI 10.1007/s10541-005-0093-4
    • Bogachev, A. V., and Verkhovsky, M. I. (2005) Na+-Translocating NADH:quinone oxidoreductase: Progress achieved and prospects of investigations. Biochemistry (Moscow, Russ. Fed.) 70, 143-149. (Pubitemid 40512320)
    • (2005) Biochemistry (Moscow) , vol.70 , Issue.2 , pp. 143-149
    • Bogachev, A.V.1    Verkhovsky, M.I.2
  • 4
    • 0028892667 scopus 로고
    • Predicted structure and possible ionmotive mechanism of the sodium-linked NADH-ubiquinone oxidoreductase of Vibrio alginolyticus
    • Rich, P. R., Meunier, B., and Ward, F. B. (1995) Predicted structure and possible ionmotive mechanism of the sodium-linked NADH-ubiquinone oxidoreductase of Vibrio alginolyticus. FEBS Lett. 375, 5-10.
    • (1995) FEBS Lett , vol.375 , pp. 5-10
    • Rich, P.R.1    Meunier, B.2    Ward, F.B.3
  • 5
    • 2442641688 scopus 로고    scopus 로고
    • +-translocating NADH:quinone oxidoreductase from Vibrio cholerae: Functional role of the NqrF subunit
    • +-translocating NADH:quinone oxidoreductase from Vibrio cholerae: Functional role of the NqrF subunit. J. Biol. Chem. 279, 21349-21355.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21349-21355
    • Turk, K.1    Puhar, A.2    Neese, F.3    Bill, E.4    Fritz, G.5    Steuber, J.6
  • 8
  • 9
    • 0035831096 scopus 로고    scopus 로고
    • + pump from Vibrio cholerae with covalently attached FMN
    • + pump from Vibrio cholerae with covalently attached FMN. FEBS Lett. 492, 45-49.
    • (2001) FEBS Lett , vol.492 , pp. 45-49
    • Barquera, B.1    Hase, C.C.2    Gennis, R.B.3
  • 12
    • 33845993613 scopus 로고    scopus 로고
    • +-pumping NADH: Quinone oxidoreductase from Vibrio cholerae: An EPR/ENDOR investigation of the role of the covalently bound flavins in subunits B and C
    • +-pumping NADH: quinone oxidoreductase from Vibrio cholerae: An EPR/ENDOR investigation of the role of the covalently bound flavins in subunits B and C. J. Biol. Chem. 281, 36482-36491.
    • (2006) J. Biol. Chem. , vol.281 , pp. 36482-36491
    • Barquera, B.1    Ramirez-Silva, L.2    Morgan, J.E.3    Nilges, M.J.4
  • 15
    • 33845468702 scopus 로고    scopus 로고
    • +-pumping NADH:quinone oxidoreductase from Vibrio cholerae by PhoA-green fluorescent protein fusion analysis
    • +-pumping NADH:quinone oxidoreductase from Vibrio cholerae by PhoA-green fluorescent protein fusion analysis. J. Bacteriol. 188, 8343-8345.
    • (2006) J. Bacteriol. , vol.188 , pp. 8343-8345
    • Duffy, E.B.1    Barquera, B.2
  • 16
    • 66649095357 scopus 로고    scopus 로고
    • Genetic, immunological and biochemical evidence for a Rnf complex in the acetogen Acetobacterium woodii
    • Biegel, E., Schmidt, S., and Muller, V. (2009) Genetic, immunological and biochemical evidence for a Rnf complex in the acetogen Acetobacterium woodii. Environ. Microbiol. 11, 1438-1443.
    • (2009) Environ. Microbiol. , vol.11 , pp. 1438-1443
    • Biegel, E.1    Schmidt, S.2    Muller, V.3
  • 17
    • 0042931286 scopus 로고    scopus 로고
    • Sequence motifs, polar interactions and conformational changes in helical membrane proteins
    • Curran, A. R., and Engelman, D. M. (2003) Sequence motifs, polar interactions and conformational changes in helical membrane proteins. Curr. Opin. Struct. Biol. 13, 412-417.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 412-417
    • Curran, A.R.1    Engelman, D.M.2
  • 21
    • 0029101114 scopus 로고
    • Reconstitution of membrane proteins into liposomes: Application to energy-transducing membrane proteins
    • Rigaud, J. L., Pitard, B., and Levy, D. (1995) Reconstitution of membrane proteins into liposomes: Application to energy-transducing membrane proteins. Biochim. Biophys. Acta 1231, 223-246.
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 223-246
    • Rigaud, J.L.1    Pitard, B.2    Levy, D.3
  • 23
    • 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
  • 24
    • 0025267390 scopus 로고
    • Potential-sensitive molecular probes in membranes of bioenergetic relevance
    • Smith, J. C. (1990) Potential-sensitive molecular probes in membranes of bioenergetic relevance. Biochim. Biophys. Acta 1016, 1-28.
    • (1990) Biochim. Biophys. Acta , vol.1016 , pp. 1-28
    • Smith, J.C.1
  • 25
    • 36549018651 scopus 로고    scopus 로고
    • Dissection of the caffeate respiratory chain in the acetogen Acetobacterium woodii: Identification of an Rnf-type NADH dehydrogenase as a potential coupling site
    • DOI 10.1128/JB.01017-07
    • Imkamp, F., Biegel, E., Jayamani, E., Buckel, W., and Muller, V. (2007) Dissection of the caffeate respiratory chain in the acetogen Acetobacterium woodii: Identification of an Rnf-type NADH dehydrogenase as a potential coupling site. J. Bacteriol. 189, 8145-8153. (Pubitemid 350178926)
    • (2007) Journal of Bacteriology , vol.189 , Issue.22 , pp. 8145-8153
    • Imkamp, F.1    Biegel, E.2    Jayamani, E.3    Buckel, W.4    Muller, V.5
  • 26
    • 0001139274 scopus 로고
    • Characterization of the sodium- Dependent respiratory chain NADH:quinone oxidoreductase of the marine bacterium, Vibrio alginolyticus, in relation to the primary sodium pump
    • Hayashi, M., and Unemoto, T. (1984) Characterization of the sodium- dependent respiratory chain NADH:quinone oxidoreductase of the marine bacterium, Vibrio alginolyticus, in relation to the primary sodium pump. Biochim. Biophys. Acta 767, 470-477.
    • (1984) Biochim. Biophys. Acta , vol.767 , pp. 470-477
    • Hayashi, M.1    Unemoto, T.2
  • 30
    • 28544453561 scopus 로고    scopus 로고
    • Principles of selective ion transport in channels and pumps
    • DOI 10.1126/science.1113666
    • Gouaux, E., and Mackinnon, R. (2005) Principles of selective ion transport in channels and pumps. Science 310, 1461-1465. (Pubitemid 41746336)
    • (2005) Science , vol.310 , Issue.5753 , pp. 1461-1465
    • Gouaux, E.1    MacKinnon, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.