STRUCTURE AND KINETICS OF FORMATION OF CATECHOL COMPLEXES OF FERRIC SOYBEAN LIPOXYGENASE-1

被引：21

作者：

NELSON, MJ ^{[1
]}

BRENNAN, BA ^{[1
]}

CHASE, DB ^{[1
]}

COWLING, RA ^{[1
]}

GROVE, GN ^{[1
]}

SCARROW, RC ^{[1
]}

机构：

[1] HAVERFORD COLL,DEPT CHEM,HAVERFORD,PA 19041

来源：

BIOCHEMISTRY | 1995年 / 34卷 / 46期

关键词：

D O I：

10.1021/bi00046a030

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：

Ferric soybean lipoxygenase forms stable complexes with 4-substituted catechols. The structure of the complex between the enzyme and 3,4-dihydroxybenzonitrile has been studied by resonance Raman, electron paramagnetic resonance, visible, and X-ray spectroscopies. It is a bidentate iron-catecholate complex with at least one water ligand. The kinetics of formation of complexes between lipoxygenase and 3,4-dihydroxybenzonitrile and 3,4-dihydroxyacetophenone have been studied by stopped-flow spectroscopy. The data are consistent with two kinetically distinct, reversible steps. The pH dependence of the first step suggests that the substrate for the reaction is the catechol monoanion. When these results are combined, plausible mechanisms for the complexation reaction are suggested.

引用

页码：15219 / 15229

页数：11

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