Precise design of artificial cofactors for enhancing peroxidase activity of myoglobin: Myoglobin mutant H64D reconstituted with a "single-winged cofactor" Is equivalent to native horseradish peroxidase in oxidation activity

Chemistry - An Asian Journal

Volumn 6, Issue 9, 2011, Pages 2491-2499

  Matsuo, Takashi ^b   Fukumoto, Kazuki ^a   Watanabe, Takuro ^a   Hayashi, Takashi ^a  

^a OSAKA UNIVERSITY   (Japan)

^b NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

cofactors; heme proteins; myoglobin; oxidation; reconstitution

Indexed keywords

2-METHOXYPHENOL; AROMATIC RINGS; COFACTORS; HEME PROPIONATES; HEME PROTEINS; HORSE-RADISH PEROXIDASE; MYOGLOBIN; OXIDATION ACTIVITIES; PEROXIDASE ACTIVITIES; RECONSTITUTION; SUBSTRATE-BINDING DOMAINS;

CARBOXYLATION; CATALYST ACTIVITY; OXIDATION; PHENOLS; PORPHYRINS; PROTEINS;

DRUG PRODUCTS;

GUAIACOL; HEME; HORSERADISH PEROXIDASE; MYOGLOBIN;

AMINO ACID SUBSTITUTION; ARTICLE; BIOCATALYSIS; CHEMISTRY; COENZYME; GENETICS; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN BINDING;

AMINO ACID SUBSTITUTION; BIOCATALYSIS; COENZYMES; GUAIACOL; HEME; HORSERADISH PEROXIDASE; MYOGLOBIN; OXIDATION-REDUCTION; PROTEIN BINDING;

EID: 80051751303     PISSN: 18614728     EISSN: 1861471X     Source Type: Journal    
DOI: 10.1002/asia.201100107     Document Type: Article

References (37)

1. P. D. Beer, P. A. Gale, D. K. Smith, in Supramolecular Chemistry, Oxford University Press, New York, 2003 and reference therein.
2. J.-M. Lehn, in Supramolecular Chemistry, Wiley-VCH, Weinheim, 1995 and references therein.
3. E. L. Raven, A. G. Mauk, in Advances in Inorganic Chemistry, Vol. 51, Academic Press, San Diego, 2000, pp. 1-49
4. T. Hayashi, Y. Hisaeda, Acc. Chem. Res. 2002, 35, 35-43
5. T. Ueno, S. Abe, N. Yokoi, Y. Watanabe, Coord. Chem. Rev. 2007, 251, 2717-2731
6. M. D. Toscano, K. J. Woycechowsky, D. Hilvert, Angew. Chem. 2007, 119, 3274-3300
7. Angew. Chem. Int. Ed. 2007, 46, 3212-3236
8. L. Fruk, J. Müller, G. Weber, A. Narváez, E. Domínguez, C. M. Niemeyer, Chem. Eur. J. 2007, 13, 5223-5231
9. Y. Lu, D. K. Garner, J.-L. Zhang, in Wiley Encyclopedia of Chemical Biology, Vol. 1 (Eds:, T. P. Begley,), Wiley, Hoboken, NJ, 2008, pp. 124-133
10. L. Fruk, C.-H. Kuo, E. Torres, C. M. Niemeyer, Angew. Chem. 2009, 121, 1578-1603
11. Angew. Chem. Int. Ed. 2009, 48, 1550-1574
12. J. Steinreiber, T. R. Ward, Coord. Chem. Rev. 2008, 252, 751-756
13. T. Matsuo, T. Hayashi, J. Porphyrins Phthalocyanines 2009, 13, 1082-1089.
14. E. Antonini, M. Brunori, in Hemoglobin and Myoglobin in Their Reaction with Ligands, North-Holland, Amsterdam, 1971.
15. T. Matsui, S. Ozaki, Y. Watanabe, J. Am. Chem. Soc. 1999, 121, 9952-9957
16. T. D. Pfister, T. Ohki, T. Ueno, I. Hara, S. Adachi, Y. Makino, N. Ueyama, Y. Lu, Y. Watanabe, J. Biol. Chem. 2005, 280, 12858-12866 and references therein.
17. I. Hamachi, T. Nagase, Y. Tajiri, S. Shinkai, Chem. Commun. 1996, 2205-2206.
18. T. Hayashi, Y. Hitomi, T. Ando, T. Mizutani, Y. Hisaeda, S. Kitagawa, H. Ogoshi, J. Am. Chem. Soc. 1999, 121, 7747-7750
19. T. Hayashi, T. Matsuda, Y. Hisaeda, Chem. Lett. 2003, 32, 496-497.
20. E. Monzani, G. Alzuet, L. Casella, C. Redaelli, C. Bassani, A. M. Sanangelantoni, M. Gullotti, L. D. Gioia, L. Santagostini, F. Chillemi, Biochemistry 2000, 39, 9571-9582.
21. S. Sakamoto, K. Kudo, Bull. Chem. Soc. Jpn. 2005, 78, 1749-1756.
22. T. Hayashi, D. Murata, M. Makino, H. Sugimoto, T. Matsuo, H. Sato, Y. Shiro, Y. Hisaeda, Inorg. Chem. 2006, 45, 10530-10536
23. T. Matsuo, D. Murata, H. Hori, Y. Hisaeda, T. Hayashi, J. Am. Chem. Soc. 2007, 129, 12906-12907.
24. T. Matsuo, A. Hayashi, M. Abe, T. Matsuda, Y. Hisaeda, T. Hayashi, J. Am. Chem. Soc. 2009, 131, 15124-15125.
25. H. Sato, T. Hayashi, T. Ando, Y. Hisaeda, T. Ueno, Y. Watanabe, J. Am. Chem. Soc. 2004, 126, 436-437.
26. K. Harada, M. Makino, H. Sugimoto, S. Hirota, T. Matsuo, Y. Shiro, Y. Hisaeda, T. Hayashi, Biochemistry 2007, 46, 9406-9416 and references therein
27. T. Hayashi, K. Harada, K. Sakurai, H. Shimada, S. Hirota, J. Am. Chem. Soc. 2009, 131, 1398-1400 and reference therein.
28. G. N. La Mar, U. Pande, J. B. Hauksson, R. K. Pandey, K. M. Smith, J. Am. Chem. Soc. 1989, 111, 485-491
29. G. N. La Mar, H. Toi, R. Krishnamoorthi, J. Am. Chem. Soc. 1984, 106, 6395-6401
30. Y. Wu, E. Y. T. Chien, S. G. Sligar, G. N. La Mar, Biochemistry 1998, 37, 6979-6990 and reference therein.
31. The X-ray structures of similar mutants, H64D/V68A and H64D/V68S Mbs, show the normal heme orientation in the heme pocket., H.-J. Yang, T. Matsui, S. Ozaki, S. Kato, T. Ueno, G. N. Phillips, Jr., S. Fukuzumi, Y. Watanabe, Biochemistry 2003, 42, 10174-10181.
32. Similar behavior was observed in Mb with a flavin-pendant hemin, in which the flavin moiety was linked to one of the two propionates., T. Matsuo, T. Hayashi, Y. Hisaeda, J. Am. Chem. Soc. 2002, 124, 11234-11235.
33. The latest report regarding product analysis of 2-methoxyphenol oxidation mediated by peroxidases proposed that 3,3′-dimethoxy-4,4′- biphenylquinone is formed as the main product., D. R. Doerge, R. L. Divi, M. I. Churchwell, Anal. Biochem. 1997, 250, 10-17.
34. M. I. Savenkova, J. M. Kuo, P. R. Ortiz de Montellano, Biochemistry 1998, 37, 10828-10836.
35. F. W. Teale, Biochim. Biophys. Acta 1959, 35, 543.
36. G. D. DePillis, B. P. Sishta, A. G. Mauk, P. R. Ortiz de Montellano, J. Biol. Chem. 1991, 266, 19334-19341
37. B. Chance, A. C. Maehly, Methods Enzymol. 1955, 2, 764-775.