Reactivities of oxo and peroxo intermediates studied by hemoprotein mutants

被引：119

作者：

Watanabe, Yoshihito ^{[1
]}

Nakajima, Hiroshi

Ueno, Takafumi

机构：

[1] Nagoya Univ, Res Ctr Mat Sci, Grad Sch Sci, Chikusa Ku, Nagoya, Aichi 4648602, Japan

[2] Nagoya Univ, Dept Chem, Grad Sch Sci, Chikusa Ku, Nagoya, Aichi 4648602, Japan

来源：

ACCOUNTS OF CHEMICAL RESEARCH | 2007年 / 40卷 / 07期

关键词：

PEROXIDASE COMPOUND-I; SITE-DIRECTED MUTAGENESIS; HYDROGEN-PEROXIDE; HORSERADISH-PEROXIDASE; MYOGLOBIN MUTANTS; OXYGEN-TRANSFER; PURIFIED CYTOCHROME-P-450; OXIDATIVE MODIFICATION; RECONSTITUTED SYSTEM; TRANSFER MECHANISM;

D O I：

10.1021/ar600046a

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A series of myoglobin mutants, in which distal sites are modified by site-directed mutagenesis, are able to catalyze peroxidase, catalase, and P450 reactions even though their proximal histidine ligands are intact. More importantly, reactions of P450, catalase, and peroxidase substrates and compound I of myoglobin mutants can be observed spectroscopically. Thus, detailed oxidation mechanisms were examined. On the basis of these results, we suggest that the different reactivities of P450, catalase, and peroxidase are mainly caused by their active site structures, but not the axial ligand. We have also prepared compound 0 under physiological conditions by employing a mutant of cytochrome c(552). Compound 0 is not able to oxidize ascorbic acid.

引用

页码：554 / 562

页数：9

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