Photoinduced oxidation of horseradish peroxidase

Journal of the American Chemical Society

Volumn 119, Issue 10, 1997, Pages 2464-2469

  Berglund, Johan ^a   Pascher, Torbjörn ^a   Winkler, Jay R ^a   Gray, Harry B ^a  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HORSERADISH PEROXIDASE;

ARTICLE; ENZYME ACTIVITY; PHOTOCHEMISTRY; SPECTROPHOTOMETRY;

EID: 0030906534     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja961026m     Document Type: Article

References (46)

1. Valentine, J. S. In Bioinorganic Chemistry; Bertini, I., Gray, H. B., Lippard, S. J., Valentine, J. S., Eds.; University Science Books: Mill Valley, CA, 1994; pp 253-315.
2. Dunford, H. B.; Stillman, J. S. Coord. Chem. Rev. 1976, 19, 187.
3. Dawson, J. H. Science 1988, 240, 433.
4. Erman, J. E.; Vitello, L. B.; Mauro, J. M.; Kraut, J. Biochemistry 1989, 28, 7992.
5. Palaniappan, V.; Terner, J. J. Biol. Chem. 1989, 264, 16046.
6. Chuang, W.-J.; Van Wart, H. E. J. Biol. Chem. 1992, 267, 13293.
7. Farhangrazi, Z. S.; Fossett, M. E.; Powers, L. S.; Ellis, W. R., Jr. Biochemistry 1995, 34, 2866.
8. George, P. Science 1953, 117, 220.
9. Fergusson, R. R. J. Am. Chem. Soc. 1956, 78, 741.
10. Hayashi, Y.; Yamazaki, I. J. Biol. Chem. 1979, 254, 9101.
11. Farhangrazi, Z. S.; Copeland, B. R.; Nakayama, T.; Amachi, T.; Yamazaki, I.; Powers, L. S. Biochemistry 1994, 33, 5647.
12. Brill, A. S. Comp. Biochem. 1966, 14, 447.
13. Hasinoff, B. B.; Dunford, H. B. Biochemistry 1970, 9, 4930.
14. Bohne, C.; MacDonald, D. I.; Dunford, H. B. J. Biol. Chem. 1987, 262, 3572.
15. Nakamura, M.; Hayashi, T. Arch. Biochem. Biophys. 1992, 299, 313.
16. Nakamura, M. J Biochem. 1991, 110, 595.
17. Kaneko, Y.; Tamura, M.; Yamazaki, I. Biochemistry 1980, 19, 5795.
18. Kuwahara, Y.; Tamura, M.; Yamazaki, I. J. Biol. Chem. 1982, 257, 11517.
19. Farhangrazi, Z. S.; Sinclair, R.; Powers, L.; Yamazaki, I. Biochemistry 1995, 34, 14970.
20. Phillippi, M. A.; Shimomura, E. T.; Goff, H. M. Inorg. Chem. 1981, 20, 1322.
21. Phillippi, M. A.; Goff, H. M. J. Am. Chem. Soc. 1982, 104, 6026.
22. Brault, D.; Neta, P. J. Phys. Chem. 1984, 88, 2857.
23. Brault, D.; Neta, P. Chem. Phys. Lett. 1985, 121, 28.
24. Marguet, S.; Hapiot, P.; Neta, P. J. Phys. Chem. 1994, 98, 7136.
25. Gans, P.; Buisson, G.; Duee, E.; Marchon, J.-C; Erler, B. S.; Scholz, W. F.; Reed, C. A. J. Am. Chem. Soc. 1986, 108, 1223.
26. Groves, J. T.; Gross, Z.; Stern, M. K. Inorg. Chem. 1994, 33, 5065.
27. Hoffman, M. Z.; Bolleta, F.; Moggi, L.; Hug, G. L. J. Phys. Chem. Ref. Data 1989, 18, 219-543.
28. Low, D. W.; Winkler, J. R.; Gray, H. B. J. Am. Chem. Soc. 1996, 118, 117.
29. Shannon, L. M.; Kay, E.; Lew, J. Y. J. Biol. Chem. 1966, 241, 2166.
30. Ohlsson, P.-I.; Paul, K.-G. Acta Chem. Scand. 1976, B30, 373.
31. Non-commercial program developed to facilitate treatment of data obtained from the laser setup.
32. -1 (ref 2), we estimate there is 98% conversion to compound II based on the spectrum shown in Figure 1.
33. Ghosh, P. K.; Brunschwig, B. S.; Chou, M.; Creutz, C.; Sutin, N. J. Am. Chem. Soc. 1984, 102, 4772.
34. s-1).
35. The scaling was done by multiplying the T spectrum (Figure 4a) by a factor that gives the same absorption at 422 nm as the L spectrum.
36. III spectrum).
37. There is a possibility that some fraction of the Ru(III) does not oxidize the porphyrin ring but rather another group of the enzyme, for example, a tyrosine residue. This oxidation would not be detectable in the Soret spectrum of the enzyme, since tyrosine radicals do not absorb strongly in this wavelength region. In this case, a smaller absorptivity would be calculated for the π-cation porphyrin radical (Figure 4b).
38. Gajhede, M. Private communication.
39. Band, L.; Carloni, P.; Savellini, G. G. Biochemistry 1994, 33, 12356.
40. Sitter, A. J.; Shifflett, J. R.; Terner, J. J. Biol. Chem. 1988, 263, 13032 and references therein.
41. Harbury, H. A. J. Biol. Chem. 1957, 225, 1009.
42. -1, which puts this reaction on the same timescale as HRPc ferryl formation at pH <9.8. King, B. C.; Hawkridge, F. M.; Huffman, B. M. J. Am. Chem. Soc. 1992, 114, 10603.
43. 3+, which is the probable reason that its oxidation is so much faster.
44. It was not possible to run experiments above pH 10.8, since both the Ru sensitizer and the Co quencher are not stable in strongly alkaline solution.
45. A second, slower reaction, with <10% of the amplitude of the main reaction, also was observed. The final difference spectrum had the same qualitative features as the difference spectrum between compound I and compound II of HRP.
46. 3+ depletion as the concentration of compound II builds up.