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Publication Abstract from PubMed

Manganese cofactors activate strong chemical bonds in many essential enzymes. Yet very few manganese-dependent enzymes are known to functionalize ubiquitous carbon-hydrogen (C-H) bonds, and those that catalyze this important reaction display limited intrinsic reactivity. Herein, we report that the 2-aminoisobutyric acid hydroxylase from Rhodococcus wratislaviensis requires manganese to functionalize a C-H bond possessing a bond dissociation enthalpy (BDE) exceeding 100 kcal/mol. Structural and spectroscopic studies of this enzyme reveal a redox-active, heterobimetallic manganese-iron active site that utilizes a manganese ion at the locus for O (2) activation and substrate coordination. Accordingly, this enzyme represents the first documented Mn-dependent monooxygenase in biology. Related proteins are widespread in microorganisms suggesting that many uncharacterized monooxygenases may utilize manganese-containing cofactors to accomplish diverse biological tasks.

Enzymatic Hydroxylation of Aliphatic C-H Bonds by a Mn/Fe Cofactor.,Powell MM, Rao G, Britt RD, Rittle J bioRxiv. 2023 Mar 11:2023.03.10.532131. doi: 10.1101/2023.03.10.532131. Preprint. PMID:36945426^[1]

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