Reaction coordinate analysis for β-diketone cleavage by the non-heme Fe2+-dependent dioxygenase Dke1

Journal of the American Chemical Society

Volumn 127, Issue 35, 2005, Pages 12306-12314

  Straganz, Grit D ^a   Nidetzky, Bernd ^a  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CATALYSIS; CHEMICAL BONDS; COMPLEXATION; COORDINATION REACTIONS; ENZYMES; FREE ENERGY; IRON; POSITIVE IONS; REACTION KINETICS;

Β-DIKETONE; 2,4-PENTANEDIONE (PD); METHYLGLYOXAL; REACTION COORDINATES;

KETONES;

1,3 DIKETONE; 2' HYDROXYACETOPHENONE; ACETIC ACID; ACETOPHENONE; ACETYLACETONE; ACETYLACETONE DIOXYGENASE; CARBON; CARBONYL DERIVATIVE; ENZYME; IRON; METHYLGLYOXAL; OXYGENASE; UNCLASSIFIED DRUG;

ACINETOBACTER; ACINETOBACTER JOHNSONII; ARTICLE; CATALYSIS; CHEMICAL BOND; CHEMICAL REACTION; ENERGY; KINETICS; REACTION ANALYSIS; REDUCTION;

ACINETOBACTER; CARBON; CHROMATOGRAPHY, GEL; DIOXYGENASES; FERROUS COMPOUNDS; KETONES; KINETICS; NONHEME IRON PROTEINS; OXIDATION-REDUCTION; OXYGEN; PROTEIN BINDING; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; SUBSTRATE SPECIFICITY;

EID: 24644510665     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja042313q     Document Type: Article

References (42)

1. (a) Straganz, G. D.; Hofer, H.; Steiner, W.; Nidetzky, B. J. Am. Chem. Soc. 2004, 126, 12202-12203.
2. (b) Straganz, G. D.; Glieder, A.; Brecker, L.; Ribbons, D. W.; Steiner, W. Biochem. J. 2003, 369, 573-581.
3. For a review, see: (a) Costas, M.; Mehn, M. P.; Jensen, M. P.; Que, L., Jr. Chem. Rev. 2004, 104, 939-986.
4. (b) Bugg, T. D. Curr. Opin. Chem. Biol. 2001, 5, 550-555.
5. (c) Solomon, E. I.; Brunold, T. C.; Davis, M. I.; Kemsley, J. N.; Lee, S. K.; Lehnert, N.; Neese, F.; Skulan, A. J.; Yang, Y. S.; Zhou, J. Chem. Rev. 2000, 100, 235-350.
6. (d) Lange, S. J.; Que, L., Jr. Curr. Opin. Chem. Biol. 1998, 2, 159-172.
7. (e) Hegg, E. L.; Que, L., Jr. Eur. J. Biochem. 1997, 250, 625-629.
8. (f) Que, L., Jr.; Ho, R. Y. Chem. Rev. 1996, 96, 2607-2624.
9. Stranzl, G. D. Ph.D. Thesis. Karl Franzens University, Graz, Austria, 2002.
10. (a) Solomon, E. I.; Decker, A.; Lehnert, N. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 3589-3594.
11. (b) Davis, M. I.; Wasinger, E. C.; Decker, A.; Pau, M. Y. M.; Vaillancourt, F. H.; Bolin, J. T.; Eltis, L. D.; Hedman, B.; Hodgson, K. O.; Solomon, E. I. J. Am. Chem. Soc. 2003, 125, 11214-11227.
12. Shan, X.; Que, L., Jr. Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 5340-5345.
13. (a) Bassan, A.; Borowski, T.; Siegbahn, P. E. M. J. Chem. Soc., Dalton Trans. 2004, 20, 3153-3162.
14. (b) Sawyer, D. T. In Oxygen Complexes and Oxygen Activation by Transition Metals; Martell, A. E., Sawyer, D. T., Eds.; Plenum: New York, 1988; pp 131-148.
15. Vaillancourt, F. H.; Labbe, G.; Drouin, N. M.; Fortin, P. D.; Eltis, L. D. J. Biol. Chem. 2002, 277, 2019-2027.
16. (a) Que, L., Jr.; Lipscomb, J. D.; Munck, E.; Wood, J. M. Biochim. Biophys. Acta 1977, 485, 60-74.
17. (b) Hamilton, G. A. In Molecular Mechanisms of Oxygen Actiuation; Hayaishi, O., Ed.; Academic Press: New York, 1974; pp 443-445.
18. Steiner, R. A.; Kalk, K. H.; Dijkstra, B. W. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 16625-16630.
19. Straganz, G. D.; Slavica, A.; Hofer, H.; Mandl, U.; Steiner, W.; Nidetzky, B. Biocatal. Biotransform., in press.
20. Johnson-Winters, K.; Purpero, V. M.; Kavana, M.; Nelson, T.; Moran, G. R. Biochemistry 2003, 42, 2072-2080.
21. Eng, S. J.; Motekaitis, R. J.; Martell, A. E. Inorg. Chim. Acta 1998, 278, 170-177.
22. (a) Ryle, M. J.; Padmakumar, R.; Hausinger, R. P. Biochemistry 1999, 38, 15278-15286.
23. (b) Hegg, E. L.; Whiting, A. K.; Saari, R. E.; McCracken, J.; Hausinger, R. P.; Que, L., Jr. Biochemistry 1999, 38, 16714-16726.
24. (a) Denisov, I. G.; Makris, T. M.; Sugar, S. G.; Schlichting, I. Chem. Rev. 2005, 105, 2253-2277.
25. (b) Ost, T. W.; Clark, J.; Mowat, C. G.; Miles, C. S.; Walkinshaw, M. D.; Reid, G. A.; Chapman, S. K.; Daff, S. J. Am. Chem. Soc. 2003, 125, 15010-15020.
26. (c) Miles, C. S.; Ost, T. W.; Noble, M. A.; Munro, A. W.; Chapman, S. K. Biochim. Biophys. Acta 2000, 1543, 383-407.
27. (d) Daff, S. N.; Chapman, S. K.; Turner, K. L.; Holt, R. A.; Govindaraj, S.; Poulos, T. L.; Munro, A. W. Biochemistry 1997, 36, 13816-13823.
28. (e) Sligar, S. G. Biochemistry 1976, 15, 5399-5406.
29. Endo, K.; Furukawa, M.; Yamatera, H.; Sano, H. Bull Chem. Soc. Jpn. 1980, 53, 407-410.
30. 3+, which is released into solution because in its oxidized form the metal has no detectable affinity for the active site. Details of the Dke1 inactivation pathway will be reported elsewhere.
31. Walsh, T. A.; Ballou, D. P. J. Biol. Chem. 1983, 258, 14413-14421.
32. (a) Ridder, L.; Briganti, F.; Boersma, M. G.; Boeren, S.; Vis, E. H.; Scozzafava, A.; Veeger, C.; Rietjens, I. M. Eur. J. Biochem. 1998, 257, 92-100.
33. (b) Walsh, T. A.; Ballou, D. P.; Mayer, R.; Que, L., Jr. J. Biol. Chem. 1983, 258, 14422-14427.
34. Grzyska, P. K.; Ryle, M. J.; Monterosso, G. R.; Liu, J.; Ballou, D. P.; Hausinger, R. P. Biochemistry 2005, 44, 3845-3855.
35. Groce, S. L.; Miller-Rodeberg, M. A.; Lipscomb, J. D. Biochemistry 2004, 43, 15141-15153.
36. 2 reduction by Dke1.
37. cat values. The conclusion is also valid for the transient rate constants.
38. 24b which otherwise share the requirement for substrate-derived electrons to drive the catalytic reaction. Choice of an appropriate substrate made it possible to uncouple superoxide production from subsequent substrate transformations catalyzed by the latter enzymes. Considering Scheme 2, similar approaches would seem to be elusive for Dke1.
39. (b) Mayer, R.; Widom, J.; Que, L., Jr. Biochem. Biophys. Res. Commun. 1980, 92, 285-291.
40. (a) Bowater, L.; Fairhurst, S. A.; Just, V. J.; Bornemann, S. FEBS Lett. 2004, 557, 45-48.
41. (b) Barney, B. M.; Schaab, M. R.; LoBrutto, R.; Francisco, W. A. Protein Expression Purif. 2004, 35, 131-141.
42. Gopal, B.; Madan, L. L.; Betz, S. F.; Kossiakoff, A. A. Biochemistry 2005, 44, 193-201.