Department of Chemistry, University of California, Berkeley, Berkeley, California 94720, United States.
Department of Chemistry, University of California, Davis, Davis, California 95616, United States.
J Am Chem Soc. 2024 Jan 24;146(3):1783-1788. doi: 10.1021/jacs.3c12131. Epub 2024 Jan 10.
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.
双核单加氧酶在自然界中介导具有挑战性的 C-H 键氧化反应。这些酶中的许多被认为专门利用二铁辅因子。在此，我们报告了一种孤立双核单加氧酶的生物信息学发现，该酶优先利用异双核锰-铁（Mn/Fe）辅因子来介导 O 依赖性 C-H 键羟化反应。与结构相似的 Mn/Fe 依赖性单加氧酶 AibH2 不同，该酶的二铁形式（SfbO）表现出初始酶活性。这种行为提出了这样一种可能性，即许多其他双核单加氧酶可能具有利用具有可变金属含量的辅因子的能力。
