A Water-soluble Supramolecular Complex That Mimics the Heme/copper Hetero-binuclear Site of Cytochrome Oxidase

Overview

Journal Chem Sci

Publisher Royal Society of Chemistry

Specialty Chemistry

Date 2018 Apr 21

PMID 29675246

Citations 5

Authors

Hiroaki Kitagishi

Daiki Shimoji

Takehiro Ohta

Ryo Kamiya

Yasuhiro Kudo

Akira Onoda

Takashi Hayashi

Jean Weiss

Jennifer A Wytko

Koji Kano

Affiliations

Soon will be listed here.

Abstract

In mitochondria, cytochrome oxidase (CO) catalyses the reduction of oxygen (O) 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 CO. A tridentate copper(ii) complex was fixed onto 5,10,15,20-tetrakis(4-sulfonatophenyl)porphinatoiron(iii) (FeTPPS) through supramolecular complexation between FeTPPS and a per--methylated β-cyclodextrin dimer linked by a (2,2':6',2''-terpyridyl)copper(ii) complex (CuTerpyCD). The reduced FeTPPS/CuTerpyCD complex reacted with O in an aqueous solution at pH 7 and 25 °C to form a superoxo-type Fe-O/Cu complex in a manner similar to CO. The pH-dependent autoxidation of the O complex suggests that water molecules gathered at the distal Cu site are possibly involved in the Fe-O/Cu superoxo complex in an aqueous solution. Electrochemical analysis using a rotating disk electrode demonstrated the role of the FeTPPS/CuTerpyCD hetero-binuclear structure in the catalytic O reduction reaction.

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