Kinetics of the spectral changes during reduction of the Na+-motive NADH:Quinone oxidoreductase from Vibrio harveyi

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1556, Issue 2-3, 2002, Pages 113-120

  Bogachev, Alexander V ^a   Bertsova, Yulia V ^a   Ruuge, Enno K ^b   Wikström, Mårten ^c   Verkhovsky, Michael I ^c  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b INSTITUTE OF EXPERIMENTAL CARDIOLOGY   (Russian Federation)

^c UNIVERSITY OF HELSINKI   (Finland)

Author keywords

Bacteria; Flavin cofactor; Na+ NADH:quinone oxidoreductase; Na+ pump; Respiratory enzyme; Vibrio harveyi

Indexed keywords

ANION; BACTERIAL ENZYME; FLAVINE ADENINE NUCLEOTIDE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SEMIQUINONE; SODIUM ION;

ARTICLE; CATALYSIS; CONTROLLED STUDY; COVALENT BOND; DEVICE; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ENZYME METABOLISM; KINETICS; NONHUMAN; PRIORITY JOURNAL; SODIUM TRANSPORT; SPECTROSCOPY; TIME; VIBRIO HARVEYI;

BACTERIAL PROTEINS; DITHIOTHREITOL; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT COMPLEX I; KINETICS; NADH, NADPH OXIDOREDUCTASES; OXIDATION-REDUCTION; SODIUM; VIBRIO; VITAMIN K 3;

VIBRIO; VIBRIO HARVEYI;

EID: 0037010878     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(02)00342-0     Document Type: Article

References (29)

1. Tokuda H., Unemoto T. A respiration-dependent primary sodium extrusion system functioning at alkaline pH in the marine bacterium Vibrio alginolyticus. Biochem. Biophys. Res. Commun. 102:1981;265-271.
2. + pump in the marine bacterium Vibrio alginolyticus. J. Biol. Chem. 257:1982;10007-10014.
3. + in α-aminoisobutyric acid transport by the marine bacterium Vibrio alginolyticus. J. Biol. Chem. 257:1982;788-794.
4. +-dependent motility and modes of membrane energization in the marine alkalotolerant Vibrio alginolyticus. Biochim. Biophys. Acta. 850:1986;449-457.
5. +-coupled oxidative phosphorylation in Vibrio alginolyticus cells. Biochim. Biophys. Acta. 850:1986;458-465.
6. + pump. Biochim. Biophys. Acta. 767:1984;470-478.
7. +-translocating NADH-quinone reductase from the marine Vibrio alginolyticus. FEBS Lett. 422:1998;240-242.
8. Rich P.R., Meunier B., Ward F.B. Predicted structure and possible ionmotive mechanism of the sodium-linked NADH-ubiquinone oxidoreductase of Vibrio alginolyticus. FEBS Lett. 375:1995;5-10.
9. +-translocating NADH-quinone reductase from Vibrio alginolyticus. FEBS Lett. 363:1995;75-77.
10. Tan K., Beattie P., Leach D.R., Rich P.R., Coulson A.F., Ward F.B. Expression and analysis of the gene for the catalytic beta subunit of the sodium-translocating NADH-ubiquinone oxidoreductase of Vibrio alginolyticus. Biochem. Soc. Trans. 24:1996;12S.
11. + pump. Biochemistry. 35:1996;6233-6242.
12. +-motive NADH:quinone oxidoreductase from Vibrio harveyi. Biochemistry. 40:2001;7318-7323.
13. +-translocating NADH:quinone oxidoreductase from Vibrio cholerae. Biochemistry. 41:2002;3781-3789.
14. +-translocating NADH:ubiquinone oxidoreductase from Vibrio alginolyticus by reactive oxygen species. Eur. J. Biochem. 269:2002;1287-1292.
15. +-translocating NADH:ubiquinone oxidoreductase from Vibrio harveyi. Biochemistry. 38:1999;16246-16252.
16. +-translocating NADH-quinone reductase from Vibrio alginolyticus. FEBS Lett. 474:2000;165-168.
17. +-translocating NADH-quinone reductase from Vibrio alginolyticus. FEBS Lett. 488:2001;5-8.
18. + pump from Vibrio cholerae with covalently attached FMN. FEBS Lett. 492:2001;45-49.
19. +-motive NADH:quinone oxidoreductase in Vibrio alginolyticus. FEBS Lett. 409:1997;475-477.
20. 3 of Escherichia coli. Biochemistry. 34:1995;15633-15637.
21. Provencher S.W., Vogel R.H. Regularization techniques for inverse problems in molecular biology. Deuflhard P., Hairer E. Progress in Scientific Computing. vol. 2:1983;304-319 Birkhauser, Boston.
22. Massey V., Palmer G. On the existence of spectrally distinct classes of flavoprotein semiquinones. A new method for the quantitative production of flavoprotein semiquinones. Biochemistry. 5:1966;3181-3189.
23. Murataliev M.B. Application of electron spin resonance (ESR) for detection and characterization of flavoprotein semiquinones. Methods Mol. Biol. 131:1999;97-110.
24. Stankovich M.T., Schopfer L.M., Massey V. Determination of glucose oxidase oxidation-reduction potentials and the oxygen reactivity of fully reduced and semiquinoid forms. J. Biol. Chem. 253:1978;4971-4979.
25. Ells A.H. A colorimetric method for the assay of soluble succinic dehydogenase and pyridinenucleotide-linked dehydrogenases. Arch. Biochem. Biophys. 85:1959;561-562.
26. 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., Klenk D.C. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150:1985;76-85.
27. Grigolava I.V., Konstantinov A.A., Ksenzenko M.I., Ruuge E.K., Tikhonov A.N. Interaction of ubisemiquinone with succinate dehydrogenase and the cytochrome chain of mitochondria. Biokhimiya. 47:1982;1970-1982.
28. G. Palmer, F. Muller, V. Massey, Electron paramagnetic resonance studies on flavoprotein radicals, in: H. Kamin (Ed.), Flavins and Flavoproteins, University Park Press and Butterworths, Baltimore and London, 1971, pp. 123-139.
29. De_Luca G., Asso M., Belaich J.P., Dermoun Z. Purification and characterization of the HndA subunit of NADP-reducing hydrogenase from Desulfovibrio fructosovorans overproduced in Escherichia coli. Biochemistry. 37:1998;2660-2665.