The cumulative electrostatic effect of aromatic stacking interactions and the negative electrostatic environment of the flavin mononucleotide binding site is a major determinant of the reduction potential for the flavodoxin from Desulfovibrio vulgaris [Hildenborough]

Biochemistry

Volumn 35, Issue 50, 1996, Pages 15980-15988

  Zhou, Zhimin ^a,b   Swenson, Richard P ^a  

^a OHIO STATE UNIVERSITY   (United States)

^b DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FLAVINE MONONUCLEOTIDE; FLAVODOXIN; MUTANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; DESULFOVIBRIO; DISSOCIATION CONSTANT; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PLASMID; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS;

BINDING SITES; DESULFOVIBRIO VULGARIS; ELECTROSTATICS; FLAVIN MONONUCLEOTIDE; FLAVODOXIN; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; POINT MUTATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; TYROSINE;

EID: 0030456586     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi962124n     Document Type: Article

References (29)

1. Anderson, R. F. (1983) Biochim. Biophys. Acta 722, 158-162.
2. Breinlinger, E., Niemz, A., & Rotello, V. (1997) in Flavins and Flavoproteins 1996 (Stevenson, K. J., Massey, V., & Williams, C. H., Jr., Eds.) University of Calgary Press, Calgary, Alberta, (in press).
3. Cammack, R., Rao, K., Hall, D., Moura, J., Xavier, A., Bruschi, M., LeGall, J., Deville, A., & Gayda, J. (1977) Biochim. Biophys. Acta 490, 311-317.
4. Connolly, M. L. (1983) Science 221, 709-712.
5. Curley, G. P., Carr, M. C., Mayhew, S. G., & Voordouw, G. (1991) Eur. J. Biochem. 202, 1091-1100.
6. D'Anna, J. R., Jr., & Tollin, G. (1972) Biochemistry 11, 1073-1080.
7. Degtyarenko, K. N. (1995) Protein Eng. 8, 737-747.
8. Deistung, J., & Thornely, R. N. F. (1988) Biochem. J. 253, 587-595.
9. Draper, R. D., & Ingraham, L. L. (1968) Arch. Biochem. Biophys. 125, 802-808.
10. Dubourdieu, M., LeGall, J., & Favaudon. V. (1975) Biochim. Biophys. Acta 376, 519-532.
11. Dutton, P., & Baltscheffsky, M. (1972) Biochim. Biophys. Acta 267, 172-178.
12. Hunter, C. A., & Sanders, J. K. M. (1990) J. Am. Chem. Soc. 112, 5525-5534.
13. Hunter, C. A., Singh, J., & Thornton, J. M. (1991) J. Mol Biol. 218, 837-846.
14. Krey, G. D., Vanin, E. F., & Swenson, R. P. (1988) J. Biol. Chem. 244, 15436-15443.
15. Kunkel, T. A. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 488-492.
16. Ludwig, M. L., & Luschinsky, C. L. (1992) in Chemistry and Biochemistry of Flavoenzymes (Müller, F., Ed.) Vol. III, pp 427-466, CRC Press, Boca Raton, FL.
17. Mayhew, S. G. (1971) Biochim. Biophys. Acta 235, 276-288.
18. Mayhew, S. G., & Tollin, G. (1992) in Chemistry and Biochemistry of Flavoenzymes (Müller, F., Ed.) Vol. III, pp 389-426, CRC Press, Boca Raton, FL.
19. Müller, F. (1992) in Chemistry and Biochemistry of Flavoenzymes (Müller, F., Ed.) Vol. I, pp 1-71, CRC Press, Boca Raton, FL.
20. Nieva-Gomez, D., Roberts, G. P., Klevickis, S., & Brill, W. J. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 2555-2558.
21. Sanger, F., Nicklen, S., & Coulson (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 5463-5467.
22. Stockman, B. J., Euvrard, A., Kloosterman, D. A., Scahill, T. A., & Swenson, R. P. (1993) J. Biomol. NMR 3, 133-149.
23. Stockman, B. J., Richardson, T. E., & Swenson R. P. (1994) Biochemistry 33, 15298-15308.
24. Swenson, R. P., & Krey, G. D. (1994) Biochemistry 33, 8505-8514.
25. Swenson, R. P., Krey, G. D., & Eren, M. (1991) in Flavins and Flavoproteins (Curti, B., Ronchi, S., & Zanetti, G., Eds.) pp 415-422, Walter de Gruyter & Co., Berlin and New York.
26. Wassink, J. H., & Mayhew, S. G. (1975) Anal. Biochem. 68, 609-616.
27. Watenpaugh, K. D., Sieker, L. C., & Jensen, L. H. (1973) Proc. Natl. Acad. Sci. U.S.A. 70, 3857-3860.
28. Watt, W., Tulinsky, A., Swenson, R. P., & Watenpauph, K. D. (1991) J. Mol. Biol. 218, 195-208.
29. Zhou, Z., & Swenson, R. P. (1995) Biochemistry 34, 3183-3192.