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The catalytic pathway of horseradish peroxidase at high resolution

journal contribution
posted on 2023-06-08, 05:40 authored by Gunnar I Berglund, Gunilla H Carlsson, Andrew T Smith, Hanna Szoke, Anette Henriksen, Janos Hajdu
A molecular description of oxygen and peroxide activation in biological systems is difficult, because electrons liberated during X-ray data collection reduce the active centres of redox enzymes catalysing these reactions(1-5). Here we describe an effective strategy to obtain crystal structures for high-valency redox intermediates and present a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP). We also describe separate experiments in which high-resolution structures could be obtained for all five oxidation states of HRP, showing such structures with preserved redox states for the first time.

History

Publication status

  • Published

Journal

Nature

ISSN

0028-0836

Volume

417

Page range

463-368

Pages

6.0

Department affiliated with

  • Biochemistry Publications

Notes

ATS contributed the recombinant HRP, spectral deconvolution expertise, co-drafted the manuscript and coordinated the funding application. First description of the x-ray structures of classical horseradish peroxidase in all five oxidation states, including the catalytically relevant Fe (IV) intermediates and first catalytic movie for dioxygen reduction, cited 157 times.

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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