Chemical Science

In mitochondria, cytochrome c oxidase (CcO) catalyses the reduction of oxygen (O₂) to water by using a heme/copper hetero-binuclear active site. Here we report a highly efficient supramolecular approach for the construction of a water-soluble biomimetic model for the active site of CcO. A tridentate copper(II) complex was fixed onto 5,10,15,20-tetrakis(4-sulfonatophenyl)porphinatoiron(III) (Fe^IIITPPS) through supramolecular complexation between Fe^IIITPPS and a per-O-methylated β-cyclodextrin dimer linked by a (2,2′:6′,2′′-terpyridyl)copper(II) complex (Cu^IITerpyCD₂). The reduced Fe^IITPPS/Cu^ITerpyCD₂ complex reacted with O₂ in an aqueous solution at pH 7 and 25 °C to form a superoxo-type Fe^III–O₂⁻/Cu^I complex in a manner similar to CcO. The pH-dependent autoxidation of the O₂ complex suggests that water molecules gathered at the distal Cu site are possibly involved in the Fe^III–O₂⁻/Cu^I superoxo complex in an aqueous solution. Electrochemical analysis using a rotating disk electrode demonstrated the role of the FeTPPS/CuTerpyCD₂ hetero-binuclear structure in the catalytic O₂ reduction reaction.

Référence :

A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase
Chem. Sci. 2018, doi:10.1039/C7SC04732K

Contact chercheur:

Jean Weiss Institut de Chimie de Strasbourg

Courriel : jweiss@unistra.fr