Bioinformatic Discovery of a Cambialistic Monooxygenase

Year: 2024

Type: article

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 nascent enzymatic activity. This behavior raises the possibility that many other dinuclear monooxygenases may be endowed with the capacity to harness cofactors with variable metal content.

Source: Journal of the American Chemical Society

DOI: 10.1021/jacs.3c12131

Authors: Chang Liu, Magan M. Powell, Guodong Rao, R. David Britt, Jonathan Rittle

Institutions: University of California, Berkeley, University of California, Davis

Language: English

Topic: Metal-Catalyzed Oxygenation Mechanisms

Subfield: Inorganic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $4,500

Funders: National Science Foundation, U.S. Department of Energy, National Institutes of Health, UC Berkeley College of Chemistry, National Institute of General Medical Sciences, Division of Graduate Education, Basic Energy Sciences

OpenAlex ID: W4390692777