8SM9

Air-oxidized C. fi TruffO expressed from M9 minimal medium supplemented with Fe

Summary for 8SM9

• Entry DOI: 10.2210/pdb8sm9/pdb
• Descriptor: Amidohydrolase 2, FE (III) ION (3 entities in total)
• Functional Keywords: oxygenase, amidohydrolase-like, pf04909, oxidoreductase
• Biological source: Cytobacillus firmus DS1
• Total number of polymer chains: 4
• Total formula weight: 167632.38

Authors

Liu, C.,Rittle, J. (deposition date: 2023-04-25, release date: 2024-03-13)

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

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)