Zinc binding to peptide analogs of the structural zinc site in alcohol dehydrogenase: Implications for an entatic state

Cellular and Molecular Life Sciences

Volumn 65, Issue 24, 2008, Pages 4019-4027

  Bergman, T ^a,b   Zhang, K ^c   Palmberg, C ^b   Jornvall H ^b   Auld, D S ^a,d  

^a HARVARD MEDICAL SCHOOL   (United States)

^b KAROLINSKA INSTITUTE   (Sweden)

^c ILLINOIS INSTITUTE OF TECHNOLOGY   (United States)

^d BOSTON COLLEGE   (United States)

Author keywords

4 (2 pyridylazo)resorcinol; Alcohol dehydrogenase; Atomic absorption; Entatic state; Synthetic peptides; X ray absorption fine structure analysis; X ray crystallography; Zinc

Indexed keywords

ALCOHOL DEHYDROGENASE; CHELATING AGENT; CYSTEINE; LIGAND; ZINC;

ARTICLE; CHROMATOGRAPHY; CONTROLLED STUDY; CRYSTAL STRUCTURE; HYDROGEN BOND; NONHUMAN; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN SYNTHESIS; STOICHIOMETRY;

ALCOHOL DEHYDROGENASE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; CATALYTIC DOMAIN; CHROMATOGRAPHY, GEL; FOURIER ANALYSIS; HORSES; KINETICS; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; TITRIMETRY; ZINC;

EQUIDAE;

EID: 58149116809     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-8379-5     Document Type: Article

References (41)

1. Vallee, B. L. and Auld, D. S. (1990) Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29, 5647-5659.
2. Auld, D. S. (2001) Zinc coordination sphere in biochemical zinc sites. Biometals 14, 271-313.
3. Auld, D. S. (2005) Zinc enzymes. In: Encyclopedia of Inorganic Chemistry, vol. IX, pp. 5885-5927, King R. B. (ed.), John Wiley & Sons, Chichester.
4. Vallee, B. L. and Hoch, F. L. (1957) Zinc in horse liver alcohol dehydrogenase. J. Biol. Chem. 225, 185-195.
5. Åkeson, Å. (1964) On the zinc content of horse liver alcohol dehydrogenase. Biochem. Biophys. Res. Commun. 17, 211-214.
6. Drum, D. E., Li, T. K. and Vallee, B. L. (1969) Considerations in evaluating the zinc content of horse liver alcohol dehydrogenase preparations. Biochemistry 8, 3783-3791.
7. Sytkowski, A. J. and Vallee, B. L. (1976) Chemical reactivities of catalytic and noncatalytic zinc or cobalt atoms of horse liver alcohol dehydrogenase: differentiation by their thermodynamic and kinetic properties. Proc. Natl. Acad. Sci. USA 73, 344-348.
8. Brändén, C.-I., Jörnvall, H., Eklund, H. and Furugren, B. (1975) Alcohol dehydrogenase. In: The Enzymes, vol. 11, pp. 103-190, Boyer P. D. (ed.), Academic Press, New York.
9. 2O of zinc enzymes. Proc. Natl. Acad. Sci. USA 87, 220-224.
10. Auld, D. S. (2004) Structural zinc sites. In: The Handbook of Metalloproteins, vol. 3, pp. 403-415, Messerschmidt, A., Bode, W. and Cygler, M. (eds.), John Wiley & Sons, Chichester.
11. Vendruscolo, M. and Dobson, C. M. (2005) A glimpse at the organization of the protein universe. Proc. Natl. Acad. Sci. USA 102, 5641-5642.
12. Eklund, H., Nordström, B., Zeppezauer, E., Söderlund, G., Ohlsson, I., Boiwe, T., Söderberg, B.-O., Tapia, O., Brändén, C.-I. and Åkeson, Å. (1976) Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution. J. Mol. Biol. 102, 27-59.
13. Jörnvall, H. (1973) Differences in thiol groups and multiple forms of rat liver alcohol dehydrogenase. Biochem. Biophys. Res. Commun. 53, 1096-1101.
14. Maret, W. and Vallee, B. L. (1998) Thiolate ligands in metallothionein confer redox activity on zinc clusters. Proc. Natl. Acad. Sci. USA 95, 3478-3482.
15. Maret, W. (2004) Zinc and sulfur: A critical biological partnership. Biochemistry 43, 3301-3309.
16. 2 human liver alcohol dehydrogenase. Eur. J. Biochem. 173, 281-285.
17. Jeffery, J., Chesters, J., Mills, C., Sadler, P. J. and Jörnvall, H. (1984) Sorbitol dehydrogenase is a zinc enzyme. EMBO J. 3, 357-360.
18. Jörnvall, H., von Bahr-Lindström, H. and Jeffery, J. (1984) Extensive variations and basic features in the alcohol dehydrogenase-sorbitol dehydrogenase family. Eur. J. Biochem. 140, 17-23.
19. Jeloková, J., Karlsson, C., Estonius, M., Jörnvall, H. and Höög, J.-O. (1994) Features of structural zinc in mammalian alcohol dehydrogenase. Site-directed mutagenesis of the zinc ligands. Eur. J. Biochem. 225, 1015-1019.
20. Bergman, T., Jörnvall, H., Holmquist, B. and Vallee, B. L. (1992)Asynthetic peptide encompassing the binding site of the second zinc atom (the 'structural' zinc) of alcohol dehydrogenase. Eur. J. Biochem. 205, 467-470.
21. Bergman, T., Palmberg, C., Jörnvall, H., Auld, D. S. and Vallee, B. L. (1999) Zinc binding characteristics of the synthetic peptide corresponding to the structural zinc site of horse liver alcohol dehydrogenase. Adv. Exp. Med. Biol. 463, 339-342.
22. Vallee, B. L. and Williams, R. J. P. (1968) Metalloenzymes: The entatic nature of their active sites. Proc. Natl. Acad. Sci. USA 59, 498-505.
23. Williams, R. J. P. (1995) Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins. Eur. J. Biochem. 234, 363-381.
24. Behnke, W. D. and Vallee, B. L. (1972) The spectrum of cobalt bovine procarboxypeptidase A, an index of catalytic function. Proc. Natl. Acad. Sci. USA 69, 2442-2445.
25. Holmquist, B. (1988) Elimination of adventitious metals. Methods Enzymol. 158, 6-12.
26. 5). Inorg. Chem. 21, 3265-3269.
27. Zhang, K., Chance, B., Auld, D. S., Larsen, K. S. and Vallee, B. L. (1992) X-ray absorption fine structure study of the active site of zinc and cobalt carboxypeptidase A in their solution and crystalline forms. Biochemistry 31, 1159-1168.
28. Zhang, K., Rosenbaum, G. and Bunker, G. (1993) The correction of the dead time loss of the Ge detector in x-ray absorption spectroscopy. Jpn J. Appl. Phys. 32 Suppl. 32-2, 147-149.
29. Zhang, K. and Auld, D. S. (1993) XAFS studies of carboxypeptidase A: Detection of a structural alteration in the zinc coordination sphere coupled to the catalytically important alkaline pKa. Biochemistry 32, 13844-13851.
30. Stern, E. A. and Heald, S. M. (1983) In: Handbook of Synchrotron Radiation, vol. 1B, pp. 955-1014, Koch, E.-E., Eastman, D. E. and Farge, Y. (eds.) North-Holland, New York.
31. Zhang, K., Stern, E. A., Ellis, F., Sanders-Loehr, J. and Shiemke, A. K. (1988) The active site of hemerythrin as determined by X-ray absorption fine structure. Biochemistry 27, 7470-7479.
32. Bunker, G., Stern, E. A., Blankenship, R. E. and Parson, W. W. (1982) An x-ray absorption study of the iron site in bacterial photosynthetic reaction centers. Biophys. J. 37, 539-551.
33. Lee, P. A., Citrin, P. H., Eisenberger, P. and Kincaid, B. M. (1981) Extended x-ray absorption fine structure - Its strengths and limitations as a structural tool. Rev. Mod. Phys. 53, 769-806.
34. Vallee, B. L. and Auld, D. S. (1989) Short and long spacer sequences and other structural features of zinc binding sites in zinc enzymes. FEBS Lett. 257, 138-140.
35. Nordling, E., Persson, B. and Jörnvall, H. (2002) Differential multiplicity of MDR alcohol dehydrogenases: enzyme genes in the human genome versus those in organisms initially studied. Cell. Mol. Life Sci. 59, 1070-1075.
36. Protein Information Resource. www-nbrf.georgetown.edu.
37. Maynard, A. T. and Covell, D. G. (2001) Reactivity of zinc finger cores: Analysis of protein packing and electrostatic screening. J. Am. Chem. Soc. 123, 1047-1058.
38. 113Cd-substituted rubredoxin from Pyrococcus furiosus. J. Am. Chem. Soc. 114, 4931-4933.
39. Smith, J. N., Hoffman, J. T., Shirin, Z. and Carrano, C. J. (2005) H-bonding interactions and control of thiolate nucleophilicity and specificity in model complexes of zinc metalloproteins. Inorg. Chem. 44, 2012-2017.
40. Britto, P. J., Knipling, L. and Wolff, J. (2002) The local electrostatic environment determines cysteine reactivity of tubulin. J. Biol. Chem. 277, 29018-29027.
41. Clark-Baldwin, K., Johnson, A. R., Chen, Y.-W., Dekker, E. E. and Penner-Hahn, J. E. (1998) Structural characterization of the zinc site in Escherichia coli L-threonine dehydrogenase using extended X-ray absorption fine structure spectroscopy. Inorg. Chim. Acta 275-276, 215-221.