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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 HajduA 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
NatureISSN
0028-0836External DOI
Volume
417Page range
463-368Pages
6.0Department 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
2012-02-06Usage metrics
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