Conversion of myoglobin into a highly stereospecific peroxygenase by the L29H/H64L mutation

Journal of the American Chemical Society

Volumn 118, Issue 40, 1996, Pages 9784-9785

  Ozaki, Shin Ichi ^a   Matsui, Toshitaka ^b   Watanabe, Yoshihito ^a,b  

^a INSTITUTE FOR MOLECULAR SCIENCE   (Japan)

^b GRADUATE UNIVERSITY FOR ADVANCED STUDIES   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MYOGLOBIN;

ARTICLE; ENZYME ACTIVITY; IN VITRO STUDY; MUTANT; PEROXIDATION;

EID: 0030001545     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja961223l     Document Type: Article

References (29)

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16. max = 409 nm) due to the absence of water iron ligation in the mutant, as previously observed in the H64V mutant (Morikis, D.; Champion, P. M.; Springer, B. A.; Egeberg, K. D.; Sliger, S. G. J. Biol. Chem. 1990, 265, 12143). The spectra for deoxy and carbonmonoxy forms of the mutants are essentially identical to those of the wild type protein. The absorption spectrum for the hydroxy complex is identical to that in the previous report. However, hydroxy forms of the Leu-29 mutants are not clearly observed possibly due to the differences in the degree of interaction between His-29 and a water molecule bound to the heme iron.
17. IV=O) radical cation species, equivalent to compound I of peroxidase. Furthermore, the ferryl formation is not the rate-determining step in the peroxygenase cycle of Mb.
18. max, the amounts of thioanisole varied.
19. 2
20. 2 was prepared by the procedure of Ortiz de Montellano (Ortiz de Montellano, P. R.; Catalano, C. E. J. biol. Chem. 1985, 260, 9265). The dichloromethane extracts of the incubation mixtures were analyzed by GC/ MS equipped with Shimazu CBP1 capillary column.
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22. max, the amounts of styrene varied.
23. The oxidation of thioanisole by L29H/H64L Mb in the presence of styrene shows the noncompetitive kinetics.
24. Reaction of wild type and L29H/H64L Mb with phenylhydrazine was carried out using the procedure of Kunze (Kunze, K. L.; Ortiz de Montellano, P. R. J. Am. Chem. Soc. 1983, 105, 422). The UV spectra of the wild type and mutant were identical, and the spectrum of σ-bonded phenyliron complex for the wild type agreed with that previously reported.
25. 2
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