HORSERADISH-PEROXIDASE .37. COMPOUND-I FORMATION FROM RECONSTITUTED ENZYME LACKING FREE CARBOXYL GROUPS AS HEME SIDE-CHAINS

被引：14

作者：

ARAISO, T ^{[1
]}

DUNFORD, HB ^{[1
]}

CHANG, CK ^{[1
]}

机构：

[1] MICHIGAN STATE UNIV,DEPT CHEM,E LANSING,MI 48824

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 90卷 / 02期

关键词：

D O I：

10.1016/0006-291X(79)91266-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recombination of apo horseradish peroxidase with 2,4 dimethyldeutero hemin and its mono- and dimethyl esters was performed. The number of free carboxyl side chains in these three hemins is 2, 1 and 0 respectively. Despite such a difference, all of these three reconstituted enzymes can react with H2O2 to produce compound I. The second order rate constants for compound I formation are 1.3 × 107 M-1s-1, 8.5 × 106 M-1s-1 and 5.9 × 106 M-1s-1. Therefore the propionate side chain of hemin has no direct role in compound I formation. © 1979.

引用

页码：520 / 524

页数：5