Experimental and Computational Evidence for the Mechanism of Intradiol Catechol Dioxygenation by Non- Heme Iron(III) Complexes
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Publication date
2014-11-24
Authors
Jastrzebski, Robin
Quesne, Matthew G.
Weckhuysen, Bert
de Visser, Sam P.
Bruijnincx, PCA
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Article
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Abstract
Catechol intradiol dioxygenation is a unique reaction catalyzed by iron-dependent enzymes and nonheme 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.
Keywords
biomimetic models, density functional theory, enzyme models, kinetics, reactivity, NONHEME IRON ENZYMES, FUNCTIONAL MODELS, CATECHOLATOIRON(III) COMPLEXES, OXYGEN-BINDING, SPIN-CROSSOVER, ACTIVE-SITES, CLEAVAGE, 1,2-DIOXYGENASE, REACTIVITY, SYSTEM
Citation
Jastrzebski, R, Quesne, M G, Weckhuysen, B M, de Visser, S P & Bruijnincx, P C A 2014, 'Experimental and Computational Evidence for the Mechanism of Intradiol Catechol Dioxygenation by Non- Heme Iron(III) Complexes', Chemistry-A European Journal, vol. 20, no. 48, pp. 15686-15691. https://doi.org/10.1002/chem.201404988