ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2018
Combined QM/MM and Monte Carlo study for redox leveling in Mn and Fe superoxide dismutase.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 5 citations in OpenAlex.
- Predicting Iron-Sulfur Cluster Redox Potentials: A Simple Model Derived from Protein Structures.ACS omega · 2025Article
- The oxidation of the [4Fe-4S] cluster of DNA primase alters the binding energies with DNA and RNA primers.Biophysical journal · 2024Article
- Initial characterization of an iron superoxide dismutase from Thermobifida fusca.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Article
- Computational Approach for Probing Redox Potential for Iron-Sulfur Clusters in Photosystem I.Biology · 2022Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
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Abstract
Superoxide dismutases (SOD) are vital enzymes for disproportionation of superoxide molecules in mammals. Despite the high similarity between the Mn-SOD and Fe-SOD, they are inactive if the metals in the active sites are exchanged. Here, we use DFT, QM/MM and Monte Carlo sampling to optimize the crystal structure and to calculate the mid-point potential for the native and substituted Mn/Fe-SOD. The optimized DFT and QM/MM structures of the Mn-SOD show a major conformational change for the conserved TYR34 compared to the X-ray structure. These changes reduce the distance between TYR34 and Mn ion to 2.59 Å, which yields a lower reduction potential for the Mn. On contrary, there is no significant difference between optimized and crystal structures in the Fe-SOD. The calculated E
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