Post-translational his-cys cross-linkage formation in tyrosinase induced by copper(II)-peroxo species

Journal of the American Chemical Society

Volumn 133, Issue 5, 2011, Pages 1180-1183

  Fujieda, Nobutaka ^a   Ikeda, Takuya ^a   Murata, Michiaki ^a   Yanagisawa, Sachiko ^b   Aono, Shigetoshi ^c   Ohkubo, Kei ^a   Nagao, Satoshi ^d   Ogura, Takashi ^b   Hirota, Shun ^d   Fukuzumi, Shunichi ^a,e   Nakamura, Yukihiro ^f   Hata, Yoji ^f   Itoh, Shinobu ^a  

^a OSAKA UNIVERSITY   (Japan)

^b UNIVERSITY OF HYOGO   (Japan)

^c OKAZAKI INSTITUTE FOR INTEGRATIVE BIOSCIENCE   (Japan)

^d NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^e Ewha Womans University   (South Korea)

^f Gekkeikan Sake Company Ltd   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AEROBIC CONDITION; ASPERGILLUS ORYZAE; AUTOCATALYTIC FORMATION; COPPER (II); CROSS-LINKAGE; DICOPPER; ENZYME ACTIVE SITES; REACTIVE INTERMEDIATE;

APOENZYME; COPPER; CYSTEINE; HISTIDINE; HISTIDYL CYSTEINYL; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; ASPERGILLUS ORYZAE; CATALYSIS; CROSS COUPLING REACTION; ENZYME ACTIVE SITE; NONHUMAN; PROTEIN CROSS LINKING; PROTEIN PROCESSING;

ASPERGILLUS ORYZAE; BIOCATALYSIS; COPPER; CROSS-LINKING REAGENTS; CYSTEINE; HISTIDINE; MODELS, MOLECULAR; MONOPHENOL MONOOXYGENASE; ORGANOMETALLIC COMPOUNDS; PROTEIN CONFORMATION; PROTEIN PROCESSING, POST-TRANSLATIONAL;

EID: 79551696309     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja108280w     Document Type: Article

References (33)

1. Okeley, N. M.; van der Donk, W. A. Chem. Biol. 2000, 7, R159-R171
2. Davidson, V. L. Biochemistry 2007, 46, 5283-5292
3. Halcrow, M. A. Angew. Chem., Int. Ed. 2001, 40, 346-349
4. Klinman, J. P.; Mu, D. Annu. Rev. Biochem. 1994, 63, 299-344
5. Ito, N.; Phillips, S. E. V.; Stevens, C.; Ogel, Z. B.; McPherson, M. J.; Keen, J. N.; Yadav, K. D. S.; Knowles, P. F. Nature 1991, 350, 87-90
6. Yoshikawa, S.; Shinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; Yamashita, E.; Inoue, N.; Yao, M.; Fei, M. J.; Libeu, C. P.; Mizushima, T.; Yamaguchi, H.; Tomizaki, T.; Tsukihara, T. Science 1998, 280, 1723-1729
7. Ostermeier, C.; Harrenga, A.; Ermler, U.; Michel, H. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 10547-10553
8. Janes, S. M.; Mu, D.; Wemmer, D.; Smith, A. J.; Kaur, S.; Maltby, D.; Burlingame, A. L.; Klinman, J. P. Science 1990, 248, 981-987
9. Wang, S. X.; Mure, M.; Medzihradszky, K. F.; Burlingame, A. L.; Brown, D. E.; Dooley, D. M.; Smith, A. J.; Kagan, H. M.; Klinman, J. P. Science 1996, 273, 1078-1084
10. Kim, M.; Okajima, T.; Kishishita, S.; Yoshimura, M.; Kawamori, A.; Tanizawa, K.; Yamaguchi, H. Nat. Struct. Biol. 2002, 9, 591-596
11. Schwartz, B.; Dove, J. E.; Klinman, J. P. Biochemistry 2000, 39, 3699-3707
12. Bollinger, J. A.; Brown, D. E.; Dooley, D. M. Biochemistry 2005, 44, 11708-11714
13. Rogers, M. S.; Baron, A. J.; McPherson, M. J.; Knowles, P. F.; Dooley, D. M. J. Am. Chem. Soc. 2000, 122, 990-991
14. Firbank, S. J.; Rogers, M. S.; Wilmot, C. M.; Dooley, D. M.; Halcrow, M. A.; Knowles, P. F.; McPherson, M. J.; Phillips, S. E. V. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 12932-12937
15. Whittaker, M. M.; Whittaker, J. W. J. Biol. Chem. 2003, 278, 22090-22101
16. Rogers, M. S.; Hurtado-Guerrero, R.; Firbank, S. J.; Halcrow, M. A.; Dooley, D. M.; Phillips, S. E. V.; Knowles, P. F.; McPherson, M. J. Biochemistry 2008, 47, 10428-10439
17. Cuff, M. E.; Miller, K. I.; van Holde, K. E.; Hendrickson, W. A. J. Mol. Biol. 1998, 278, 855-870
18. Klabunde, T.; Eicken, C.; Sacchettini, J. C.; Krebs, B. Nat. Struct. Biol. 1998, 5, 1084-1090
19. Halaouli, S.; Asther, M.; Sigoillot, J. C.; Hamdi, M.; Lomascolo, A. J. Appl. Microbiol. 2006, 100, 219-232
20. Lerch, K. J. Biol. Chem. 1982, 257, 6414-6419
21. Obata, H.; Ishida, H.; Hata, Y.; Kawato, A.; Abe, Y.; Akao, T.; Akita, O.; Ichishima, E. J. Biosci. Bioeng. 2004, 97, 400-405
22. Solomon, E. I.; Sundaram, U. M.; Machonkin, T. E. Chem. Rev. 1996, 96, 2563-2605
23. 2-binding (Figure S5A [ SI ]).
24. Ling, J. S.; Nestor, L. P.; Czernuszewicz, R. S.; Spiro, T. G.; Fraczkiewicz, R.; Sharma, K. D.; Loehr, T. M.; Sanders-Loehr, J. J. Am. Chem. Soc. 1994, 116, 7682-7691
25. Henson, M. J.; Mahadevan, V.; Stack, T. D. P.; Solomon, E. I. Inorg. Chem. 2001, 40, 5068-5069
26. Baldwin, M. J.; Root, D. E.; Pate, J. E.; Fujisawa, K.; Kitajima, N.; Solomon, E. I. J. Am. Chem. Soc. 1992, 114, 10421-10431
27. Jolley, R. L.; Mason, H. S.; Evans, L. H. Biochem. Biophys. Res. Commun. 1972, 46, 878-884
28. Burns, J. A.; Butler, J. C.; Moran, J.; Whitesides, G. M. J. Org. Chem. 1991, 56, 2648-2650
29. In the crystal structures of Octopus hemocyanin (PDB code: 1JS8, Cys2549-Cys2559) and sweet potato catechol oxidase (PDB code: 1BT3, Cys27-Cys89), which have also His-Cys cross-linkage, there is a disulfide bond near the copper center (within 10 Å distance).
30. 2 indicates that the reduction step from dicopper(II) to dicopper(I) is rate limiting in the overall reaction. In fact, aeration of WT reconstituted with 2 equiv of copper(I) significantly accelerated the formation of met-WT (more than 100-fold acceleration, see Figure S8 [ SI ]).
31. Morpurgo, L.; Finazziagro, A.; Rotilio, G.; Mondovì, B. Eur. J. Biochem. 1976, 64, 453-457
32. Lu, Y.; Lacroix, L. B.; Lowery, M. D.; Solomon, E. I.; Bender, C. J.; Peisach, J.; Roe, J. A.; Gralla, E. B.; Valentine, J. S. J. Am. Chem. Soc. 1993, 115, 5907-5918
33. Lu, Y.; Gralla, E. B.; Roe, J. A.; Valentine, J. S. J. Am. Chem. Soc. 1992, 114, 3560-3562