Copper(II) and zinc(II) dinuclear enzymes model compounds: The nature of the metal ion in the biological function

Author(s)

Ferraresso, L. G. ^[1] ; de Arruda, E. G. R. ^[1] ; de Moraes, T. P. L. ^[2] ; Fazzi, R. B. ^[3] ; Ferreira, A. M. Da Costa ^[3] ; Abbehausen, C. ^[1]

Affiliation

^[1] Univ Estadual Campinas, UNICAMP, Inst Chem, POB 6154, BR-13083970 Campinas, SP - Brazil

^[2] Univ Estadual Campinas, UNICAMP, Pharmaceut Sci Coll, POB 6029, BR-13083659 Campinas, SP - Brazil

^[3] Univ Sao Paulo, Inst Chem, BR-05508000 Sao Paulo, SP - Brazil

• Document type: Journal article
• Source: Journal of Molecular Structure; v. 1150, p. 316-328, DEC 15 2017.
• Web of Science Citations: 3

Abstract

First series transition metals are used abundantly by nature to perform catalytic transformations of several substrates. Furthermore, the cooperative activity of two proximal metal ions is common and represents a highly efficient catalytic system in living organisms. In this work three dinuclear mu-phenolate bridged metal complexes were prepared with copper(II) and zinc(II), resulting in a ZnZn, CuCu and CuZn with the ligand 2-ethylaminodimethylamino phenol (saldman) as model compounds of superoxide dismutase (CuCu and CuZn) and metallo-beta-lactamases (ZnZn). Metals are coordinated in a {[}mu-phenolate bridged symmetric system. Cu(II) presents a more distorted structure, while zinc is very symmetric. For this reason, {[}CuCu(saldman)] shows higher water solubility and also higher lability of the bridge. The antioxidant and hydrolytic beta-lactamase-like activity of the complexes were evaluated. The lability of the bridge seems to be important for the antioxidant activity and is suggested to because of {[}CuCu(saldman)] presents a lower antioxidant capacity than {[}CuZn(saldman)], which showed to present a more stable bridge in solution. The hydrolytic activity of the bimetallic complexes was assayed using nitrocefin as substrate and showed {[}ZnZn(saldman)] as a better catalyst than the Cu(II) analog. The series demonstrates the importance of the nature of the metal center for the biological function and how the reactivity of the model complex can be modulated by coordination chemistry. (C) 2017 Elsevier B.V. All rights reserved. (AU)

• FAPESP's process: 15/09905-1 - Fighting bacterial resistance: are coordination compounds an options for the metallo-beta-lactamase inhibition?
• Grantee: Camilla Abbehausen
• Support Opportunities: Regular Research Grants