A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase.

ABSTRACT: 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 t

SUBMITTER: Kitagishi H 

PROVIDER: S-EPMC5892347 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature