9BU9
Mixed-valent (2/3) dimanganese SfbO
Summary for 9BU9
| Entry DOI | 10.2210/pdb9bu9/pdb |
| Descriptor | Amidohydrolase family protein, GLYCEROL, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | monooxygenase, amidohydrolase-related oxygenase, oxidoreductase |
| Biological source | Litorilinea aerophila |
| Total number of polymer chains | 4 |
| Total formula weight | 171556.70 |
| Authors | Liu, C.,Rittle, J. (deposition date: 2024-05-16, release date: 2025-08-27, Last modification date: 2026-03-11) |
| Primary citation | Liu, C.,Rao, G.,Nguyen, J.,Britt, R.D.,Rittle, J. O 2 Activation and Enzymatic C-H Bond Activation Mediated by a Dimanganese Cofactor. J.Am.Chem.Soc., 147:2148-2157, 2025 Cited by PubMed Abstract: Dioxygen (O) is a potent oxidant used by aerobic organisms for energy transduction and critical biosynthetic processes. Numerous metalloenzymes harness O to mediate C-H bond hydroxylation reactions, but most commonly feature iron or copper ions in their active site cofactors. In contrast, many manganese-activated enzymes─such as glutamine synthetase and isocitrate lyase─perform redox neutral chemical transformations and very few are known to activate O or C-H bonds. Here, we report that the dimanganese-metalated form of the cambialistic monooxygenase SfbO (Mn-SfbO) can efficiently mediate enzymatic C-H bond hydroxylation. The activity of the dimanganese form of SfbO toward substrate hydroxylation is comparable to that of its heterobimetallic Mn/Fe form but exhibits distinct kinetic profiles. Kinetic, spectroscopic, and structural studies invoke a mixed-valent dimanganese cofactor (MnMn) in O activation and evidence a stoichiometric role for superoxide in maturing an O-inert Mn cofactor. Computational studies support a hypothesis wherein superoxide addition to the Mn cofactor installs a critical bridging hydroxide ligand that stabilizes higher-valent manganese oxidation states. These findings establish the viability of proteinaceous dimanganese cofactors in mediating complex, multistep redox transformations. PubMed: 39741465DOI: 10.1021/jacs.4c16271 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.39 Å) |
Structure validation
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