Roles of Zinc Ion and Reduced Coenzyme in Horse Liver Alcohol Dehydrogenase Catalysis. The Mechanism of Aldehyde Activation

Biochemistry

Volumn 14, Issue 14, 1975, Pages 3176-3182

  Dunn, Michael F ^a   Biellmann, Jean Francois ^b   Branlant, Guy ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITÉ DE STRASBOURG   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; ZINC;

HORSE; IN VITRO STUDY; LIVER; THEORETICAL STUDY;

ALCOHOL OXIDOREDUCTASES; ALDEHYDES; ANIMAL; BINDING SITES; ENZYME ACTIVATION; HORSES; HYDROGEN-ION CONCENTRATION; KINETICS; LIVER; NAD; OXIDATION-REDUCTION; PROTEIN BINDING; SPECTROPHOTOMETRY; SPECTROPHOTOMETRY, ULTRAVIOLET; SUPPORT, U.S. GOV'T, NON-P.H.S.; TEMPERATURE; ZINC;

EID: 0016715270     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00685a022     Document Type: Article

References (29)

1. Bender, M. L., and Zerner, B. (1961), J. Am. Chem. Soc. 83, 2391.
2. Benesi, H. H., and Hildebrand, J. H. (1949), J. Am. Chem. Soc. 71, 2703.
3. Bernhard, S. A., Lau, S. J., and Noller, H. F. (1965), Biochemistry 4, 1108.
4. Biellmann, J.-F., and Jung, M. J. (1971), Eur. J. Biochem. 19, 130.
5. Brándén, C.-I., Eklund, H., Nordstrom, B., Boiwe, T., Soderlund, G., Zeppezauer, E., Ohlsson, I., and Ákeson, Á. (1973), Proc. Natl. Acad. Sci. U.S.A. 70, 2439.
6. Brooks, R. L., Shore, J. D., and Gutfreund, H. (1972), J. Biol. Chem. 247, 2382.
7. Dalziel, K. (1957), Acta Chem. Scand. 11, 396.
8. Dunn, M. F., and Hutchison, J. S. (1973), Biochemistry 12, 4882.
9. Eigen, M., and de Maeyer, L. (1963), in Investigations of Rates and Mechanisms of Reactions, Vol. VIII, Part II, Friess, S. L., Lewis, E. S., and Weissberger, A., Ed., New York, N.Y., Interscience, p 896.
10. Eklund, H., Nordstrom, B., Zeppezauer, E., Sóderlund, G., Ohlsson, L, Boiwe, T., and Brándén, C.-I. (1974), FEBS Lett. 44, 200.
11. Erman, J. E., and Hammes, G. G. (1966), Rev. Sci. Instrum. 37, 746.
12. Hope, H. (1969), Acta Crystallogr. 25, 78.
13. Karle, I. L. (1961), Acta Crystallogr. 14, 497.
14. Koyama, H. (1963), Z. Kristallogr., Kristallgeom., Kristallphys., Kristallchem. 116, 51.
15. Lee, R. T., and McElroy, W. D. (1971), Arch Biochem. Biophys. 145, 78.
16. Malhotra, O. P., and Bernhard, S. A. (1968), J. Biol. Chem. 243, 1243.
17. Malhotra, O. P. and Bernhard, S. A. (1973), Proc. Natl. Acad. Sci. U.S.A. 70, 2077.
18. Santi, D. V., McHenry, C. S., and Sommer, H. (1974), Biochemistry 13, 471.
19. Shore, J. D., Gutfreund, H., Brooks, R. L., Santiago, D., and Santiago, P. (1974), Biochemistry 13, 4185.
20. Sund, H., and Theorell, H. (1962), Enzymes 7, 26.
21. Taniguchi, S., Theorell, H., and Ákeson, Á. (1967), Acta Chem. Scand. 21, 1903.
22. Theorell, H., and McKinley-McKee, J. S. (1961), Acta Chem. Scand. 5, 1105.
23. Theorell, H., and Winer, A. D. (1959), Arch. Biochem. Biophys. 83, 291.
24. Theorell, H., and Yonetani, T. (1963), Biochem. Z. 338, 537.
25. Van Holde, K. E. (1971), Physical Biochemistry, Englewood Cliffs, N.J., Prentice-Hall, pp 57-62.
26. Walsh, C. T., Schonbrunn, A., and Abies, R. H. (1971), J. Biol. Chem. 246, 6855.
27. Wang, J. H. (1968), Science 161, 328.
28. Wilkens, R. G. (1964), Inorg. Chem. 3, 520.
29. Wilkens, R. G., and Eigen, M. (1964), Adv. Chem. Ser. No. 49, 55-80.