Calcium‐Ion Binding Mediates the Reversible Interconversion of Cis and Trans Peroxido Dicopper Cores.

Vargo, Natasha P.; Harland, Jill B.; Musselman, Bradley W.; Lehnert, Nicolai; Ertem, Mehmed Z.; Robinson, Jerome R.

Coupled dinuclear copper oxygen cores (Cu2O2) featured in type III copper proteins (hemocyanin, tyrosinase, catechol oxidase) are vital for O2 transport and substrate oxidation in many organisms. μ‐1,2‐cis peroxido dicopper cores (CP) have been proposed as key structures in the early stages of O2 binding in these proteins; their reversible isomerization to other Cu2O2 cores are directly relevant to enzyme function. Despite the relevance of such species to type III copper proteins and the broader interest in the properties and reactivity of bimetallic CP cores in biological and synthetic systems, the properties and reactivity of CP Cu2O2 species remain largely unexplored. Herein, we report the reversible interconversion of μ‐1,2‐trans peroxido (TP) and CP dicopper cores. CaII mediates this process by reversible binding at the Cu2O2 core, highlighting the unique capability for metal‐ion binding events to stabilize novel reactive fragments and control O2 activation in biomimetic systems.

COPPER proteins; CARRIER proteins; HEMOCYANIN; PHENOL oxidase; PROTEIN binding; BIOLOGICAL systems; CATECHOL; AMINE oxidase

Angewandte Chemie, 2021, Vol 133, Issue 36, p19989

0044-8249

Academic Journal

10.1002/ange.202105421