The first catalytic tyrosinase model system based on a mononuclear copper(I) complex: Kinetics and mechanism

Angewandte Chemie - International Edition

Volumn 49, Issue 36, 2010, Pages 6438-6442

  Rolff, Malte ^a   Schottenheim, Julia ^a   Peters, Gerhard ^a   Tuczek, Felix ^a  

^a UNIVERSITY OF KIEL   (Germany)

Author keywords

Bioinorganic chemistry; Enzymes; Homogeneous catalysis

Indexed keywords

BIOINORGANIC CHEMISTRY; COPPER COMPLEXES; ENZYMATIC REACTION; HOMOGENEOUS CATALYSIS; KINETICS AND MECHANISM; MODEL SYSTEM; MONONUCLEAR COPPER; PHENOL HYDROXYLATION;

BIOCHEMISTRY; CATALYSIS; CATALYSTS; ENZYMES; OXYGENATION; PHENOLS; REACTION KINETICS;

COPPER COMPOUNDS;

2 TERT BUTYL 4 QUINONE; 2,4 DI(TERT BUTYL)PHENOL; 2,4-DI-TERT-BUTYLPHENOL; 2-TERT-BUTYL-4-QUINONE; BENZOQUINONE DERIVATIVE; COORDINATION COMPOUND; COPPER; MONOPHENOL MONOOXYGENASE; PHENOL DERIVATIVE;

ARTICLE; BIOCATALYSIS; BIOLOGICAL MODEL; CHEMISTRY; KINETICS; METABOLISM;

BENZOQUINONES; BIOCATALYSIS; COORDINATION COMPLEXES; COPPER; KINETICS; MODELS, BIOLOGICAL; MONOPHENOL MONOOXYGENASE; PHENOLS;

EID: 77956037499     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201000973     Document Type: Article

References (38)

1. E. I. Solomon, U. M. Sundaram, T. E. Machonkin, Chem. Rev. 1996, 96, 2563.
2. Á. Sánchez-Ferrer, J. N. Rodríguez-López, F. García-Cánovas, F. García-Carmona, Biochim. Biophys. Acta Prot. Struct. Mol. Enzym. 1995, 1247, 1.
3. K. E. van Holde, K. I. Miller, H. Decker, J. Biol. Chem. 2001, 276, 15563.
4. Y. Matoba, T. Kumagai, A. Yamamoto, H. Yoshitsu, M. Sugiyama, J. Biol. Chem. 2006, 281, 8981.
5. H. Decker, T. Schweikardt, F. Tuczek, Angew. Chem. 2006, 118, 4658
6. Angew. Chem. Int. Ed. 2006, 45, 4546.
7. C. Eicken, C. Gerdemann, B. Krebs in Handbook of Metalloproteins, Vol. 2 (Eds.: A. Messerschmidt, R. Huber, T. Poulos, K. Wieghardt), Wiley, New York, 2001, p. 1319.
8. L. Que Jr. , W. B. Tolman, Nature 2008, 455, 333.
9. E. A. Lewis, W. B. Tolman, Chem. Rev. 2004, 104, 1047.
10. L. M. Mirica, X. Ottenwaelder, T. D. P. Stack, Chem. Rev. 2004, 104, 1013.
11. L. Q. Hatcher, K. D. Karlin, J. Biol. Inorg. Chem. 2004, 9, 669.
12. G. Battaini, A. Granata, E. Monzani, M. Gullotti, L. Casella, Adv. Inorg. Chem. 2006, 58, 185.
13. S. Itoh in Comprehensive Coordination Chemistry II, Vol. 8 (Eds.: L. Que, Jr., W. B. Tolman), Elsevier, Amsterdam, 2004, pp. 369.
14. K. D. Karlin, J. C. Hayes, Y. Gultneh, R. W. Cruse, J. W. Mckown, J. P. Hutchinson, J. Zubieta, J. Am. Chem. Soc. 1984, 106, 2121.
15. P. L. Holland, K. R. Rodgers,W. B. Tolman, Angew. Chem. 1999, 111, 1210
16. Angew. Chem. Int. Ed. 1999, 38, 1139.
17. H. Ohi, Y. Tachi, S. Itoh, Inorg. Chem. 2006, 45, 10825.
18. O. Sander, A. Henss, C. Näther, C. Würtele,M. C. Holthausen, S. Schindler, F. Tuczek, Chem. Eur. J. 2008, 14, 9714.
19. K. D. Karlin, S. Kaderli, A. D. Zuberbühler, Acc. Chem. Res. 1997, 30, 139.
20. L. Casella, M. Gullotti, R. Radaelli, P. Digennaro, J. Chem. Soc. Chem. Commun. 1991, 1611.
21. L. M. Mirica, M. Vance, D. J. Rudd, B. Hedman, K. O. Hodgson, E. I. Solomon, T. D. P. Stack, Science 2005, 308, 1890.
22. S. Itoh, H. Kumei, M. Taki, S. Nagatomo, T. Kitagawa, S. Fukuzumi, J. Am. Chem. Soc. 2001, 123, 6708.
23. M. Réglier, C. Jorand, B. Waegell, J. Chem. Soc. Chem. Commun. 1990, 1752.
24. S. Palavicini, A. Granata, E. Monzani, L. Casella, J. Am. Chem. Soc. 2005, 127, 18031.
25. B. T. Op't Holt, M. A. Vance, L. M. Mirica, D. E. Heppner, T. D. P. Stack, E. I. Solomon, J. Am. Chem. Soc. 2009, 131, 6421.
26. A. Company, S. Palavicini, I. Garcia-Bosch, R. Mas-Ballesté, L. Que Jr. , E. V. Rybak-Akimova, L. Casella, X. Ribas, M. Costas, Chem. Eur. J. 2008, 14, 3535.
27. J. E. Bulkowski, US patent 4545937, 1984.
28. M. Réglier, E. Amadéi, E. H. Alilou, F. Eydoux, M. Pierrot, B. Waegell in Bioinorganic Chemistry of Copper (Eds.: K. D. Karlin, Z. Tyeklár), Chapman & Hall, London, 1993, p 348.
29. G. Battaini, M. De Carolis, E. Monzani, F. Tuczek, L. Casella, Chem. Commun. 2003, 726.
30. A. J. Canty, N. J. Minchin, Aust. J. Chem. 1986, 39, 1063.
31. G. J. H. Buisman, P. C. J. Kamer, P.W. N. M. van Leeuwen, Tetrahedron: Asymmetry 1993, 4, 1625.
32. 2 and amine (Ref. ) and thus is induced by the HCl quench and not by the catalytic reaction.
33. L. Casella, E. Monzani, Inorg. Chem. 1996, 35, 7516.
34. The catecholate is converted into quinone through the addition of protons in the HCl quench.
35. T. Plenge, R. Dillinger, L. Santagostini, L. Casella, F. Tuczek, Z. Anorg. Allg. Chem. 2003, 629, 2258.
36. T. Osako, K. Ohkubo, M. Taki, Y. Tachi, S. Fukuzumi, S. Itoh, J. Am. Chem. Soc. 2003, 125, 11027.
37. For Glu236 in Ipomoea batatas catecholoxidase a role in deprotonating the substrate has also been proposed: C. Eicken, C. Krebs, J. C. Sacchettini, Curr. Opin. Struct. Biol. 1999, 9, 677.
38. H. Decker, F. Tuczek, unpublished result.