8SMA
SfbO with di-Manganese cofactor
Summary for 8SMA
Entry DOI | 10.2210/pdb8sma/pdb |
Descriptor | Amidohydrolase family protein, SULFATE ION, MANGANESE (II) ION, ... (4 entities in total) |
Functional Keywords | monooxygenase, amidohydrolase-like, pf04909, oxidoreductase |
Biological source | Litorilinea aerophila |
Total number of polymer chains | 4 |
Total formula weight | 170815.98 |
Authors | |
Primary citation | Liu, C.,Powell, M.M.,Rao, G.,Britt, R.D.,Rittle, J. Bioinformatic Discovery of a Cambialistic Monooxygenase. J.Am.Chem.Soc., 146:1783-1788, 2024 Cited by PubMed Abstract: Dinuclear monooxygenases mediate challenging C-H bond oxidation reactions throughout nature. Many of these enzymes are presumed to exclusively utilize diiron cofactors. Herein we report the bioinformatic discovery of an orphan dinuclear monooxygenase that preferentially utilizes a heterobimetallic manganese-iron (Mn/Fe) cofactor to mediate an O-dependent C-H bond hydroxylation reaction. Unlike the structurally similar Mn/Fe-dependent monooxygenase AibH2, the diiron form of this enzyme (SfbO) exhibits a nascent enzymatic activity. This behavior raises the possibility that many other dinuclear monooxygenases may be endowed with the capacity to harness cofactors with a variable metal content. PubMed: 38198693DOI: 10.1021/jacs.3c12131 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.18 Å) |
Structure validation
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