The European Physical Journal Special Topics

, Volume 227, Issue 14, pp 1657–1664 | Cite as

Copper coordination in formylglycine generating enzymes

  • Sonia Álvarez-Barcia
  • Johannes Kästner
Regular Article
Part of the following topical collections:
  1. Particle Methods in Natural Science and Engineering


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.


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Copyright information

© EDP Sciences, Springer-Verlag GmbH Germany, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Institute for Theoretical Chemistry, University of StuttgartStuttgartGermany

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