Mimicking the Cu Active Site of Lytic Polysaccharide Monooxygenase Using Monoanionic Tridentate N-Donor Ligands

Caitlin J Bouchey; Dimitar Y Shopov; Aaron D Gruen; William B Tolman

doi:10.1021/acsomega.2c04432

Mimicking the Cu Active Site of Lytic Polysaccharide Monooxygenase Using Monoanionic Tridentate N-Donor Ligands

ACS Omega. 2022 Sep 23;7(39):35217-35232. doi: 10.1021/acsomega.2c04432. eCollection 2022 Oct 4.

Authors

Caitlin J Bouchey¹, Dimitar Y Shopov², Aaron D Gruen¹, William B Tolman²

Affiliations

¹ Department of Chemistry, University of Minnesota, 207 Pleasant St. SE, Minneapolis, Minnesota 55455, United States.
² Department of Chemistry, Washington University in St. Louis, One Brookings Drive, Campus Box 1134, St. Louis, Missouri 63130, United States.

Abstract

In an effort to prepare small molecule mimics of the active site of lytic polysaccharide monooxygenase (LPMO), three monoanionic tridentate N donor ligands comprising a central deprotonated amide group flanked by two neutral donors were prepared, and their coordination chemistry with Cu(I) and Cu(II) was evaluated. With Cu(I), a dimer formed, which was characterized by X-ray crystallography and NMR spectroscopy. A variety of mononuclear and dinuclear Cu(II) species with a range of auxiliary ligands (MeCN, Cl^-, OH^-, OAc^-, OBz^-, CO₃ ^2-) were prepared and characterized by X-ray diffraction and various spectroscopies (UV-vis, EPR). The complexes exhibit structural similarities to the LPMO active site.

Grants and funding

R01 GM047365/GM/NIGMS NIH HHS/United States