Magnetic field effects and radical pair mechanisms in enzymes: A reappraisal of the horseradish peroxidase system

被引：27
|
作者：
Jones, Alex R.
Scrutton, Nigel S.
Woodward, Jonathan R.
机构：
[1] Univ Leicester, Dept Chem, Leicester LE1 7RH, Leics, England
[2] Univ Manchester, Fac Life Sci, Manchester M60 1QD, Lancs, England
来源：
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2006年 / 128卷 / 26期
关键词：
D O I：
10.1021/ja060463q
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Reinvestigation by stopped-flow spectrophotometry of the previously observed influence of a static magnetic field on the horseradish peroxidase (HRP)-catalyzed reduction of hydrogen peroxide by Taraban et al. (J. Am. Chem. Soc. 1997, 119, 5768) did not reproduce the originally observed effects. No magnetic field effect was observed for static fields of up to 75 mT. Field-induced changes in both k1 and k2 reported in the original work were found to produce equal and opposite effects on the shape of the observed kinetic decay of the 418 nm spectroscopic signal as a result of the difference in the relative absorbances of Native HRP and Compound II. Copyright © 2006 American Chemical Society.
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收藏
页码：8408 / 8409
页数：2
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