8sm6

Publication Abstract from PubMed

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(2)-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.

Bioinformatic Discovery of a Cambialistic Monooxygenase.,Liu C, Powell MM, Rao G, Britt RD, Rittle J J Am Chem Soc. 2024 Jan 24;146(3):1783-1788. doi: 10.1021/jacs.3c12131. Epub 2024 , Jan 10. PMID:38198693^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.