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Summary
| Description |
English: The mechanism is derived from direct visualization of atom positions, including those of protons. Catalysis utilizes an unusually deprotonated glutamine at its amide nitrogen as well as histidine and tyrosine residues that change in protonation states during enzymatic activity. |
| Date | |
| Source | Azadmanesh, J., Lutz, W.E., Coates, L. et al. Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase. Nat Commun 12, 2079 (2021). https://doi.org/10.1038/s41467-021-22290-1 |
| Author | Azadmanesh, J., Lutz, W.E., Coates, L. et al. Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase. Nat Commun 12, 2079 (2021). https://doi.org/10.1038/s41467-021-22290-1 |
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 16:41, 19 April 2021 |  | 10,000 × 4,500 (3.38 MB) | Jarjarbinks98 | Uploaded a work by Azadmanesh, J., Lutz, W.E., Coates, L. et al. Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase. Nat Commun 12, 2079 (2021). https://doi.org/10.1038/s41467-021-22290-1 from Azadmanesh, J., Lutz, W.E., Coates, L. et al. Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase. Nat Commun 12, 2079 (2021). https://doi.org/10.1038/s41467-021-22290-1 with UploadWizard |
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