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Bioinformatic Discovery of a Cambialistic Monooxygenase.


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 O2-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.

SUBMITTER: Liu C 

PROVIDER: S-EPMC10811679 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature

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Bioinformatic Discovery of a Cambialistic Monooxygenase.

Liu Chang C   Powell Magan M MM   Rao Guodong G   Britt R David RD   Rittle Jonathan J  

Journal of the American Chemical Society 20240110 3


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<sub>2</sub>-dependent C-H bond hydroxylation reaction. Unlike the structurally similar Mn/Fe-dependent monooxygenase AibH2, the diiron form of this enzym  ...[more]

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