Reduction of dopamine β-monooxygenase: A unified model for apparent negative cooperativity and fumarate activation

Journal of Biological Chemistry

Volumn 271, Issue 42, 1996, Pages 26032-26043

  Wimalasena, Kandatege ^a   Dharmasena, Silpadipathialage ^a   Wimalasena, D Shyamali ^a   Hughbanks Wheaton, Dianna K ^a  

^a WICHITA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBIC ACID DERIVATIVE; DOPAMINE; DOPAMINE BETA MONOOXYGENASE; FUMARIC ACID; N,N DIMETHYL 1,4 PHENYLENEDIAMINE; NEUROTRANSMITTER; NORADRENALIN;

ARTICLE; BINDING AFFINITY; DOPAMINERGIC SYSTEM; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SUBSTRATE; MATHEMATICAL MODEL; MEMBRANE BINDING; NEUROTRANSMISSION; PH; PRIORITY JOURNAL; STEADY STATE;

ANTICARCINOGENIC AGENTS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DOPAMINE BETA-HYDROXYLASE; ENZYME ACTIVATION; FUMARATES; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, CHEMICAL; PHENYLENEDIAMINES;

EID: 0029909758     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.42.26032     Document Type: Article

References (32)

1. Winkler, H., Hortnagl, H., and Smith, A. D. (1970) Biochem. J. 118, 303-310
2. Sabban, E. L., Greene, L. A., and Goldstein, M. (1983) J. Biol. Chem. 258, 7812-7818
3. Slater, E. P., Zaremba, S., and Hogue-Angeletti, R. A. (1981) Arch. Biochem. Biophys. 211, 288-296
4. Ingebretsen, O. C., Terland, O., and Flatmark, T. (1980) Biochim. Biophys. Acta 628, 182-189
5. Phillips, J. H. (1982) Neuroscience 7, 1595-1609
6. Huyghe, B. G., and Klinman, J. P. (1991) J. Biol. Chem. 266, 11544-11550
7. Wimalasena, K., and Wimalasena, D. S. (1995) J. Biol. Chem. 270, 27516-27524
8. Ljones, T., and Skotland, T. (1984) in Copper Proteins and Copper Enzymes (Lontie, R., ed) Vol. 2, pp. 131-157, CRC Press, Boca Raton, FL
9. Stewart, L. C., and Klinman, J. P. (1988) Annu. Rev. Biochem. 57, 551-592
10. Skotland, T., and Ljones, T. (1979) Inorg. Prospect. Biol. Med. 2, 151-180
11. Wimalasena, K., Dharmasena, S., and Wimalasena, D. S. (1994) Biochem. Biophys. Res. Commun. 200, 113-119
12. Wimalasena, K., Wimalasena, D. S. (1991) Biochem. Biophys. Res. Commun. 175, 920-927
13. Wimalasena, K., and Wimalasena, D. S. (1991) Anal. Biochem. 197, 353-361
14. Brenner, M. C., and Klinman, J. P. (1989) Biochemistry 28, 4664-4670
15. Stewart, L. C., and Klinman, J. P. (1991) J. Biol. Chem. 266, 11537-11543
16. Goldstein, M., Joh, H. T., and Garvey, T. Q., III (1968) Biochemistry 7, 2724-2730
17. Levin, E. Y., Lovenberg, B., Kaufman, S. (1960) J. Biol. Chem. 235, 2080-2086
18. Craine, J. E., Daniels, G. H., and Kaufman, S. (1973) J. Biol. Chem. 248, 7838-7844
19. Ahn, N., and Klinman, J. P. (1983) Biochemistry 22, 3096-3106
20. Ljones, T., Skotland, T., and Flatmark, T. (1976) Eur. J. Biochem. 6, 525-533
21. Kirshner, N. (1962) J. Biol. Chem. 237, 2311-2317
22. Njus, D., and Radda, G. K. (1979) Biochem. J. 180, 579-585
23. Cleland, W. W. (1979) Methods Enzymol. 63, 103-138
24. Alberty, R. A., Massey, V., Frieden, C., and Fuhlbrigge, A. R. (1954) J. Am. Chem. Soc. 76, 2485-2493
25. Michaelis, L., Schubert, M. P., and Granick, S. (1939) J. Am. Chem. Soc. 61, 1981-1982
26. Rao, P. S., and Hayon, E. (1975) J. Phys. Chem. 79, 1063-1066
27. Villafranca, J. J. (1981) in Copper Proteins (Spiro, T., ed) Vol. 3, pp. 263-289, Wiley, New York
28. Njus, D., Knoth, J., Cook, C., and Kelley, P. M. (1983) J. Biol. Chem. 258, 27-30
29. Kelley, D. M., and Njus, D. (1986) J. Biol. Chem. 261, 6429-6432
30. Wakefield, L. M., Cass, A. E. G., and Radda, G. K. (1986) J. Biol. Chem. 261, 9739-9745
31. Beers, M. F., Johnson, R. G., and Scarpa, A. (1986) J. Biol. Chem. 261, 2529-2535
32. Fersht, A. (1984) in Enzyme Structure and Mechanism, 2nd Ed., pp. 263-290, W. H. Freeman, New York