ArticleActa crystallographica. Section F, Structural biology communications2022
Cryotrapping peroxide in the active site of human mitochondrial manganese superoxide dismutase crystals for neutron diffraction.
Article in Acta crystallographica. Section F, Structural biology communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- The curious life of human mitochondrial SOD2.International journal of biological macromolecules · 2026Review
- The role of Tyr34 in proton coupled electron transfer and product inhibition of manganese superoxide dismutase.Nature communications · 2025Article
- Revealing the atomic and electronic mechanism of human manganese superoxide dismutase product inhibition.Nature communications · 2024Article
- The role of Tyr34 in proton-coupled electron transfer of human manganese superoxide dismutase.Research square · 2024Article
- Revealing the atomic and electronic mechanism of human manganese superoxide dismutase product inhibition.Research square · 2024Article
- Perfect Crystals: microgravity capillary counterdiffusion crystallization of human manganese superoxide dismutase for neutron crystallography.NPJ microgravity · 2023Article
- Cryo neutron crystallography demonstrates influence of RNA 2'-OH orientation on conformation, sugar pucker and water structure.Nucleic acids research · 2022Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Structurally identifying the enzymatic intermediates of redox proteins has been elusive due to difficulty in resolving the H atoms involved in catalysis and the susceptibility of ligand complexes to photoreduction from X-rays. Cryotrapping ligands for neutron protein crystallography combines two powerful tools that offer the advantage of directly identifying hydrogen positions in redox-enzyme intermediates without radiolytic perturbation of metal-containing active sites. However, translating cryogenic techniques from X-ray to neutron crystallography is not straightforward due to the large crystal volumes and long data-collection times. Here, methods have been developed to visualize the evasive peroxo complex of manganese superoxide dismutase (MnSOD) so that all atoms, including H atoms, could be visualized. The subsequent cryocooling and ligand-trapping methods resulted in neutron data collection to 2.30 Å resolution. The P6
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Registered trials
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