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

doi:10.1021/ja060463q

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 journal › Article › peer-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 language	English
Pages (from-to)	8408-8409
Number of pages	1
Journal	Journal of the American Chemical Society
Volume	128
Issue number	26
DOIs	https://doi.org/10.1021/ja060463q
Publication status	Published - 5 Jul 2006

Research Beacons, Institutes and Platforms

Photon Science Institute

Access to Document

10.1021/ja060463q

Cite this

@article{ab1856fbc40c4fa88c343725a23bb3aa,

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

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 {\textcopyright} 2006 American Chemical Society.",

author = "Jones, \{Alex R.\} and Scrutton, \{Nigel S.\} and Woodward, \{Jonathan R.\}",

year = "2006",

month = jul,

day = "5",

doi = "10.1021/ja060463q",

language = "English",

volume = "128",

pages = "8408--8409",

journal = "Journal of the American Chemical Society",

issn = "0002-7863",

publisher = "American Chemical Society",

number = "26",

}

TY - JOUR

T1 - Magnetic field effects and radical pair mechanisms in enzymes: A reappraisal of the horseradish peroxidase system

AU - Jones, Alex R.

AU - Scrutton, Nigel S.

AU - Woodward, Jonathan R.

PY - 2006/7/5

Y1 - 2006/7/5

N2 - 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.

AB - 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.

U2 - 10.1021/ja060463q

DO - 10.1021/ja060463q

M3 - Article

SN - 0002-7863

VL - 128

SP - 8408

EP - 8409

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 26

ER -

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

Abstract

Research Beacons, Institutes and Platforms

Access to Document

Fingerprint

Cite this