Copper coordination in formylglycine generating enzymes
Institute for Theoretical Chemistry, University of Stuttgart, Pfaffenwaldring 55, 70569 Stuttgart, Germany
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Received in final form: 26 October 2018
Published online: 8 March 2019
Formylglycine generating enzyme is a copper and oxygen-dependent protein, which catalyzes C–H activation, namely the transformation of peptidyl cysteine to formylglycine. No crystal structures of the enzyme containing copper were published so far. Here, we show by combinations of density functional theory with force fields in the QM/MM approach how copper can be incorporated in the enzyme based on two crystal structures containing Ag(I) and Cd(II) in place of Cu(I) and Cu(II). While we find a linear coordination for Cu(I) and a distorted octahedral environment for Cu(II) we also find the possibility of tetrahedral coordinations in both cases. This structural flexibility may allow the enzyme to catalyze the redox process and accommodate copper in both oxidation states.
© EDP Sciences, Springer-Verlag GmbH Germany, part of Springer Nature, 2019