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

Alex R. Jones, Nigel S. Scrutton, Jonathan R. Woodward

    Research output: Contribution to journalArticlepeer-review

    Abstract

    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.
    Original languageEnglish
    Pages (from-to)8408-8409
    Number of pages1
    JournalJournal of the American Chemical Society
    Volume128
    Issue number26
    DOIs
    Publication statusPublished - 5 Jul 2006

    Research Beacons, Institutes and Platforms

    • Photon Science Institute

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