Determining the oxidation state of elements by X-ray crystallography.

SpReAD metalloproteins oxidoreductases photoreduction radiation damage redox reactions spatially resolved anomalous dispersion refinement sulerythrin

Journal

Acta crystallographica. Section D, Structural biology
ISSN: 2059-7983
Titre abrégé: Acta Crystallogr D Struct Biol
Pays: United States
ID NLM: 101676043

Informations de publication

Date de publication:
01 Feb 2022
Historique:
received: 15 09 2021
accepted: 08 12 2021
entrez: 1 2 2022
pubmed: 2 2 2022
medline: 5 4 2022
Statut: ppublish

Résumé

Protein-mediated redox reactions play a critical role in many biological processes and often occur at centres that contain metal ions as cofactors. In order to understand the exact mechanisms behind these reactions it is important to not only characterize the three-dimensional structures of these proteins and their cofactors, but also to identify the oxidation states of the cofactors involved and to correlate this knowledge with structural information. The only suitable approach for this based on crystallographic measurements is spatially resolved anomalous dispersion (SpReAD) refinement, a method that has been used previously to determine the redox states of metals in iron-sulfur cluster-containing proteins. In this article, the feasibility of this approach for small, non-iron-sulfur redox centres is demonstrated by employing SpReAD analysis to characterize Sulfolobus tokodaii sulerythrin, a ruberythrin-like protein that contains a binuclear metal centre. Differences in oxidation states between the individual iron ions of the binuclear metal centre are revealed in sulerythrin crystals treated with H

Identifiants

pubmed: 35102889
pii: S2059798321013048
doi: 10.1107/S2059798321013048
pmc: PMC8805299
doi:

Substances chimiques

Iron-Sulfur Proteins 0
Metalloproteins 0
Hydrogen Peroxide BBX060AN9V

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

238-247

Subventions

Organisme : Deutsche Forschungsgemeinschaft
ID : 390540038

Informations de copyright

open access.

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Auteurs

Frank Lennartz (F)

Macromolecular Crystallography, Helmholtz-Zentrum Berlin, Albert-Einstein-Strasse 15, 12489 Berlin, Germany.

Jae Hun Jeoung (JH)

Department of Biology, Humboldt-Universität zu Berlin, 10099 Berlin, Germany.

Stefan Ruenger (S)

Department of Biology, Humboldt-Universität zu Berlin, 10099 Berlin, Germany.

Holger Dobbek (H)

Department of Biology, Humboldt-Universität zu Berlin, 10099 Berlin, Germany.

Manfred S Weiss (MS)

Macromolecular Crystallography, Helmholtz-Zentrum Berlin, Albert-Einstein-Strasse 15, 12489 Berlin, Germany.

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Classifications MeSH