Jastrzebski Robin, Quesne Matthew G, Weckhuysen Bert M, de Visser Sam P, Bruijnincx Pieter C A
Inorganic Chemistry and Catalysis, Debye Institute for Nanomaterials Science, Utrecht University, Universiteitsweg 99, 3584 CG Utrecht (The Netherlands); The Manchester Institute for Biotechnology and the School of Chemical Engineering and Analytical Science, The University of Manchester, 131 Princess Street, Manchester, M1 7DN (UK).
Chemistry. 2014 Nov 24;20(48):15686-91. doi: 10.1002/chem.201404988. Epub 2014 Oct 16.
Catechol intradiol dioxygenation is a unique reaction catalyzed by iron-dependent enzymes and non-heme iron(III) complexes. The mechanism by which these systems activate dioxygen in this important metabolic process remains controversial. Using a combination of kinetic measurements and computational modelling of multiple iron(III) catecholato complexes, we have elucidated the catechol cleavage mechanism and show that oxygen binds the iron center by partial dissociation of the substrate from the iron complex. The iron(III) superoxide complex that is formed subsequently attacks the carbon atom of the substrate by a rate-determining C-O bond formation step.
儿茶酚间二酚双加氧酶催化反应是一种由铁依赖性酶和非血红素铁（III）配合物催化的独特反应。在这个重要的代谢过程中，这些体系激活双氧的机制仍存在争议。通过结合动力学测量和多种儿茶酚铁（III）配合物的计算模型，我们阐明了儿茶酚裂解机制，并表明氧通过底物从铁配合物的部分解离与铁中心结合。随后形成的铁（III）超氧化物配合物通过限速的C-O键形成步骤攻击底物的碳原子。
