ArticleActa crystallographica. Section F, Structural biology communications2018
Redox manipulation of the manganese metal in human manganese superoxide dismutase for neutron diffraction.
Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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.
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Who cites it
8 citing papers in PubMed.
- The curious life of human mitochondrial SOD2.International journal of biological macromolecules · 2026Review
- 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
- Cryotrapping peroxide in the active site of human mitochondrial manganese superoxide dismutase crystals for neutron diffraction.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase.Nature communications · 2021Article
- The Role of Reactive Oxygen Species in Arsenic Toxicity.Biomolecules · 2020Review
- Neutron crystallographic study of heterotrimeric glutamine amidotransferase CAB.Acta crystallographica. Section F, Structural biology communications · 2019Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Human manganese superoxide dismutase (MnSOD) is one of the most significant enzymes in preventing mitochondrial dysfunction and related diseases by combating reactive oxygen species (ROS) in the mitochondrial matrix. Mitochondria are the source of up to 90% of cellular ROS generation, and MnSOD performs its necessary bioprotective role by converting superoxide into oxygen and hydrogen peroxide. This vital catalytic function is conducted via cyclic redox reactions between the substrate and the active-site manganese using proton-coupled electron transfers. Owing to protons being difficult to detect experimentally, the series of proton transfers that compose the catalytic mechanism of MnSOD are unknown. Here, methods are described to discern the proton-based mechanism using chemical treatments to control the redox state of large perdeuterated MnSOD crystals and subsequent neutron diffraction. These methods could be applicable to other crystal systems in which proton information on the molecule in question in specific chemical states is desired.
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