8SM6

Aerobic, Diiron(III)-metalated SfbO

Summary for 8SM6

Entry DOI	10.2210/pdb8sm6/pdb
Descriptor	Amidohydrolase family protein, SULFATE ION, FE (III) ION, ... (4 entities in total)
Functional Keywords	monooxygenase, amidohydrolase, non-heme iron, oxidoreductase
Biological source	Litorilinea aerophila
Total number of polymer chains	4
Total formula weight	170823.23
Authors	Liu, C.,Powell, M.M.,Rittle, J. (deposition date: 2023-04-25, release date: 2024-01-24, Last modification date: 2024-01-31)
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: 38198693 DOI: 10.1021/jacs.3c12131 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.39 Å)

Structure validation