Peroxide-utilizing biocatalysts: Structural and functional diversity of heme-containing enzymes

Current Opinion in Chemical Biology

Volumn 8, Issue 2, 2004, Pages 127-132

  Matsunaga, Isamu ^a   Shiro, Yoshitsugu ^b  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

^b RIKEN HARIMA INSTITUTE   (Japan)

Author keywords

Chloroperoxidase; CPO; Cytochrome P450; Horseradish peroxidase; HRP; P450; P450 SP ; P450BS ; Peroxygenase P450 from Bacillus subtilis; Peroxygenase P450 from Sphingomonas paucimobilis; TMB

Indexed keywords

CATALASE; CYTOCHROME P450; ENZYME; HEMOPROTEIN; PEROXIDE; PEROXYGENASE P450; PORPHYRIN; UNCLASSIFIED DRUG;

BIOCATALYST; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STRUCTURE; MOLECULAR DYNAMICS; PEROXIDATION; REVIEW;

HEMEPROTEINS; MOLECULAR STRUCTURE; PEROXIDASES; PEROXIDES; PROTEIN ENGINEERING;

ARMORACIA RUSTICANA; BACILLUS SUBTILIS; SPHINGOMONAS; SPHINGOMONAS PAUCIMOBILIS;

EID: 1842426962     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2004.01.001     Document Type: Review

References (34)

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32. BSβ using TMB. This peroxidase activity is coupled with peroxygenase activity, in which a peroxidase substrate and a peroxygenase substrate use the common highly reactive intermediate in a competitive manner. Molecular engineering and utilization of a deuterium-substituted fatty acid substrate enhanced the peroxidase activity and conversely greatly reduced peroxygenase activity. It should be noted that peroxidase activity was not found in the absence of the fatty acid substrate, indicating the formation of a highly reactive intermediate supported by a fatty acid substrate. If the fatty acid substrate cannot be attacked by this reactive intermediate, TMB can capture it more efficiently, resulting in enhancement in peroxidase activity.
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34. Yang H.J., Matsui T., Ozaki S., Kato S., Ueno T., Phillips G.N. Jr., Fukuzumi S., Watanabe Y. Molecular engineering of myoglobin: influence of residue 68 on the rate and the enantioselectivity of oxidation reactions catalyzed by H64D/V68X myoglobin. Biochemistry. 42:2003;10174-10181 Myoglobin is basically a carrier protein of molecular oxygen, but has little peroxidase and peroxygenase activities. However, the authors investigated the molecular engineering of this hemoprotein to improve such activities. Interestingly, the substitution of His64 with Asp successfully improved both peroxidase and peroxygenase activities. In addition, further substitution of Val68 of the His64Glu mutant with Leu improved peroxygenase activity and showed a higher enantioselectivity. The replacement of Val68 affected enantioselectivity, suggesting that this residue interacts with thioanisol, a substrate.