Analysis of the oxidation-reduction potentials of recombinant ferredoxin-NADP+ reductase from spinach chloroplasts

European Journal of Biochemistry

Volumn 239, Issue 3, 1996, Pages 662-667

  Corrado, Mario E ^a,b   Aliverti, Alessandro ^a   Zanetti, Giuliana ^a   Mayhew, Stephen G ^a,b  

^a UNIVERSITY OF MILAN   (Italy)

^b UNIVERSITY COLLEGE DUBLIN   (Ireland)

Author keywords

FAD; Flavin hydroquinone anion; Flavoprotein; Redox potential; Spinach ferredoxin NADP+ reductase

Indexed keywords

FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; RECOMBINANT PROTEIN;

ABSORPTION SPECTROSCOPY; ARTICLE; CHLOROPLAST; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME ISOLATION; NONHUMAN; OXIDATION REDUCTION POTENTIAL; POTENTIOMETRY; PRIORITY JOURNAL; SPINACH;

SPINACIA OLERACEA;

EID: 0029957852     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0662u.x     Document Type: Article

References (32)

1. Aliverti, A., Jansen, T., Zanetti, G., Ronchi, S., Herrmann, R. G. & Curti, B. (1990) Expression in Escherichia coli ferredoxin:NADP′ reductase from spinach, Eur. J. Biochem. 191, 551-555.
2. Aliverti, A., Corrado, M. E. & Zanetti, G. (1994) Involvement of lysine-88 of spinach ferredoxin-NADP′ reductase in the interaction with ferredoxin, FEBS Lett. 343, 247-250.
3. Aliverti, A., Bruns, C. M., Pandini, V. E., Karplus, P. A., Vanoni, M. A., Curti, B. & Zanetti, G. (1995) The Involvement of Ser96 in the catalytic mechanism of ferredoxin-NADP′ reductase: structure-function relationship as studied by site-directed mutagenesis and X-ray crystallography, Biochemistry 34, 8371-8379.
4. Anderson, R. F. (1983) Energetics of the one-electron reduction steps of riboflavin, FMN and FAD to their fully reduced forms, Biochim. Biophys. Acta 722, 158-162.
5. Batie, C. J. &. Kamin, H. (1981) The relation of pH and oxidation-reduction potential to the association state of the ferredoxin/ferredoxin-NADP′ reductase complex, J. Biol. Chem. 256, 7756-7763.
6. Batie, C. J. & Kamin, H. (1984) Electron transfer by ferredoxin:NADP′ reductase, J. Biol. Chem. 259, 11976-11985.
7. Batie, C. J. & Kamin, H. (1986) Association of ferredoxin-NADP′ reductase with NADP(H). Specificity and oxidation-reduction properties, J. Biol. Chem. 261, 11214-11223.
8. Bruns, C. M. & Karplus, P. A. (1995) Refined crystal structure of spinach ferredoxin reductase at 1.7 Å resolution: oxidized, reduced and 2′-phospho-5′-AMP bound states. J. Mol. Biol. 247, 125-145.
9. Clark, W. M. (1960) Oxidation-reduction potentials of organic systems. The Williams & Wilkins Company, Baltimore.
10. Corrado, M. E., Zanetti, G. & Mayhew, S. G. (1996) The redox potentials of flavodoxin from Desulfovibrio vulgaris and ferredoxin-NADP′ reductase from Spinacia oleracea and their complexes, Biochem. Soc. Trans. 24, 28S.
11. Draper, R. D. & Ingraham, L. Y. (1968) A potentiometric study of the flavin semiquinone equilibrium. Arch. Biochem. Biophys. 125, 802-808.
12. Foust, G. P., Mayhew, S. G. & Massey, V. (1969) Complex formation between ferredoxin TPN reductase and electron transfer proteins, J. Biol. Chem. 244, 964-970.
13. Fukuyama, K., Matsubara, H. & Rogers, L. J. (1992) Crystal structure of oxidized flavodoxin from a red alga Chondrus crispus refined at 1.8 Å resolution, J. Mol. Biol. 225, 775-789.
14. Ghisla, S., Massey, V., Lloste, J. M. & Mayhew, S. G. (1974) Fluorescence and optical characteristics of reduced flavins and flavoproteins, Biochemistry 13, 589-597.
15. Karplus, P. A., Daniels, M. J. & Herriott, J. R. (1991) Atomic structure of ferredoxin-NADP′ reductase: prototype for a structurally novel flavoenzyme family. Science 251, 60-66.
16. Keirns, J. J. & Wang, J. H. (1972) Studies on nicotinamide adenine dinucleotide phosphate reductase of spinach chloroplasts, J. Biol. Chem. 247, 7374-7382.
17. Lowe, H. J. & Clark, W. M. (1956) Studies on oxidation-reduction. XXIV. Oxidation-reduction potentials of flavin adenine dinucleotide, J. Biol. Chem. 221, 983-992.
18. Ludwig, M. L. & Luschinsky, C. L. (1992) Structure and redox properties of clostridial flavodoxin, in Chemistry and biochemistry of flavoenzymes (Müller, F., ed.) vol. 3, pp. 427-466, CRC Press, Boca Raton.
19. Massey, V. & Hemmerich, P. (1980) Active-site probes of flavoproteins. Biochem. Soc. Trans. 8, 246-257.
20. Mayhew, S. G., O'Connell, D. P., O'Farrell, P. A., Yalloway, G. N. & Geoghegan, S. M. (1996) Regulation of the redox potentials of flavodoxins: modification of the flavin binding site, Biochem. Soc. Trans. 24, 122 127.
21. Mayhew, S. G. & Tollin, G. (1992) General properties of flavodoxins, in Chemistry and biochemistry of flavoenzymes (Müller, F., ed.) vol. 3, pp. 386-426, CRC Press, Boca Raton.
22. Orellano, E. G., Calcaterra, N. B., Carrillo, N. & Ceccarelli, E. A. (1993) Probing the role of the carboxyl-terminal region of ferredoxin-NADP′ reductase by site-directed mutagenesis and deletion analysis, J. Biol. Chem. 268, 19267-19273.
23. Peelen, S. & Vervoort, J. (1994) Two-dimensional NMR studies of the flavin binding site of Desulfovibrio vulgaris in its three redox states, Arch. Biochem. Biophys. 314, 291-300.
24. Pueyo, J. J., Gómez-Moreno, C. & Mayhew, S. G. (1991) Oxidation-reduction potentials of ferredoxin-NADP′ reductase and flavodoxin from Anabaena PCC 7119 and their electrostatic and covalent complexes, Eur. J. Biochem. 202, 1065-1071.
25. Smith, J. M., Smith, W. H. & Knaff, D. B. (1981) Electrochemical titrations of a ferredoxin-ferredoxin:NADP′ oxidoreductase complex, Biochim. Biophys. Acta 635, 405-411.
26. Stankovich, M. T. (1980) An anaerobic spectroelectrochemical cell for studying the spectral and redox properties of flavoproteins, Anal. Biochem. 109, 295-308.
27. Swenson, R. P. & Krey, G. D. (1994) Site-directed mutagenesis of tyrosine-98 in the flavodoxin from Desulfovibrio vulgaris (Hildenborough): regulation of oxidation-reduction properties of the bound FMN cofactor by aromatic, solvent, and electrostatic interaction, Biochemistry 33, 8505-8514.
28. Watt, W., Tulinsky, A., Swenson, R. P. & Watenpaugh, K. D. (1991) Comparison of the crystal structures of a flavodoxin in its three oxidation states at cryogenic temperatures, J. Mol. Biol. 218, 195-208.
29. Yalloway, G. N., O'Connell, D. P. & Mayhew, S. G. (1996) The effects of pH on the absorption spectrum of the hydroquinone of flavodoxin from Desulfovibrio vulgaris, Biochem. Soc. Trans. 24, 24S.
30. Zanetti, G. & Aliverti, A. (1991) Ferredoxin:NADP′ oxidoreductase, in Chemistry and biochemistry of flavoenzymes (Müller, F., ed.) vol. 2, pp. 305-315, CRC Press, Boca Raton.
31. Zanetti, G. & Curti, B. (1982) Interactions of ferredoxin-NADP′ reductase with one- and two-electron carriers, in Flavins and flavoproteins (Massey, V. & Williams, C. H., eds) pp. 667-671, Elsevier/North-Holland, New York.
32. Zanetti, G., Cidaria, D. & Curti, B. (1982) Preparation of apoprotein from spinach ferredoxin-NADP′ reductase, Eur. J. Biochem. 126, 453-458.