ArticleThe Journal of biological chemistry2013
Rapid X-ray photoreduction of dimetal-oxygen cofactors in ribonucleotide reductase.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- Hydroxo-bridged active site of flavodiiron NO reductase revealed by NRVS and DFT.Proceedings of the National Academy of Sciences of the United States of America · 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
- Structural and electronic modulations of lytic polysaccharide monooxygenase (LPMO) upon chitin binding: insights from X-ray spectroscopy.Chemical science · 2025Article
- Innovative Strategies in X-ray Crystallography for Exploring Structural Dynamics and Reaction Mechanisms in Metabolic Disorders.Journal of personalized medicine · 2024Review
- Structure of a ribonucleotide reductase R2 protein radical.Science (New York, N.Y.) · 2023Article
- Catabolic Reductive Dehalogenase Substrate Complex Structures Underpin Rational Repurposing of Substrate Scope.Microorganisms · 2020Article
- Chemical flexibility of heterobimetallic Mn/Fe cofactors: R2lox and R2c proteins.The Journal of biological chemistry · 2019Article
- Redox-induced structural changes in the di-iron and di-manganese forms of Bacillus anthracis ribonucleotide reductase subunit NrdF suggest a mechanism for gating of radical access.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Copper mediated amyloid-β binding to Transthyretin.Scientific reports · 2018Article
- Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.Chemical reviews · 2018Review
- Unprecedented (μ-1,1-Peroxo)diferric Structure for the Ambiphilic Orange Peroxo Intermediate of the Nonheme N-Oxygenase CmlI.Journal of the American Chemical Society · 2017Article
- Towards characterization of photo-excited electron transfer and catalysis in natural and artificial systems using XFELs.Faraday discussions · 2016Article
- X-ray absorption spectroscopic characterization of the diferric-peroxo intermediate of human deoxyhypusine hydroxylase in the presence of its substrate eIF5a.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Structural Basis for Oxygen Activation at a Heterodinuclear Manganese/Iron Cofactor.The Journal of biological chemistry · 2015Article
- Metalloprotein structures at ambient conditions and in real-time: biological crystallography and spectroscopy using X-ray free electron lasers.Current opinion in structural biology · 2015Review
- Light-dependent production of dioxygen in photosynthesis.Metal ions in life sciences · 2015Review
- Assembly of nonheme Mn/Fe active sites in heterodinuclear metalloproteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Review
- Methods development for diffraction and spectroscopy studies of metalloenzymes at X-ray free-electron lasers.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Review
- The Mn₄Ca photosynthetic water-oxidation catalyst studied by simultaneous X-ray spectroscopy and crystallography using an X-ray free-electron laser.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Article
- Mn4Ca cluster in photosynthesis: where and how water is oxidized to dioxygen.Chemical reviews · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prototypic dinuclear metal cofactors with varying metallation constitute a class of O2-activating catalysts in numerous enzymes such as ribonucleotide reductase. Reliable structures are required to unravel the reaction mechanisms. However, protein crystallography data may be compromised by x-ray photoreduction (XRP). We studied XPR of Fe(III)Fe(III) and Mn(III)Fe(III) sites in the R2 subunit of Chlamydia trachomatis ribonucleotide reductase using x-ray absorption spectroscopy. Rapid and biphasic x-ray photoreduction kinetics at 20 and 80 K for both cofactor types suggested sequential formation of (III,II) and (II,II) species and similar redox potentials of iron and manganese sites. Comparing with typical x-ray doses in crystallography implies that (II,II) states are reached in <1 s in such studies. First-sphere metal coordination and metal-metal distances differed after chemical reduction at room temperature and after XPR at cryogenic temperatures, as corroborated by model structures from density functional theory calculations. The inter-metal distances in the XPR-induced (II,II) states, however, are similar to R2 crystal structures. Therefore, crystal data of initially oxidized R2-type proteins mostly contain photoreduced (II,II) cofactors, which deviate from the native structures functional in O2 activation, explaining observed variable metal ligation motifs. This situation may be remedied by novel femtosecond free electron-laser protein crystallography techniques.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.