ArticleActa crystallographica. Section D, Structural biology2022
Determining the oxidation state of elements by X-ray crystallography.
Article in Acta crystallographica. Section D, Structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- OAngewandte Chemie (International ed. in English) · 2026Article
- Electronic and Structural Heterogeneity in the Diiron Center of Sulerythrin: Insights From Hybrid QM/MM Calculations.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Article
- Occupancy Determination from Resonant X-ray Diffraction.Inorganic chemistry · 2025Article
- Utilizing anomalous signals for element identification in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2024Article
- High-confidence placement of low-occupancy fragments into electron density using the anomalous signal of sulfur and halogen atoms.Acta crystallographica. Section D, Structural biology · 2024Article
- A database overview of metal-coordination distances in metalloproteins.Acta crystallographica. Section D, Structural biology · 2024Article
- Fast, automated, continuous energy scans for experimental phasing at the BioMAX beamline.Journal of synchrotron radiation · 2023Article
- Structural and electronic properties of the active site of [ZnFe] SulE.Frontiers in molecular biosciences · 2022Article
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5 authors at 2 institutions in 1 country.
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Abstract
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
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