THE CATALYTIC ACTIVITY OF HUMAN MYOGLOBIN IS ENHANCED BY A SINGLE ACTIVE-SITE MUTATION - F43Y

被引：13

作者：

LEVINGER, DC ^{[1
]}

STEVENSON, JA ^{[1
]}

WONG, LL ^{[1
]}

机构：

[1] UNIV OXFORD, INORGAN CHEM LAB, OXFORD OX1 3QR, ENGLAND

来源：

JOURNAL OF THE CHEMICAL SOCIETY-CHEMICAL COMMUNICATIONS | 1995年 / 22期

关键词：

D O I：

10.1039/c39950002305

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Phenylalanine-43 in the haem pocket of human myoglobin has been replaced by tyrosine using site-directed mutagenesis: the tyrosine-43 mutant is approximately 25 times more active than the wild-type protein in mediating the oxidation of styrene by hydrogen peroxide, and gives a 96:4 ratio of R/S styrene oxide (60% of products) in contrast to the racemate (46% of products) produced by the wild-type.

引用

页码：2305 / 2306

页数：2

共 14 条

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