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A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase.
- Source :
-
Chemical science [Chem Sci] 2018 Jan 15; Vol. 9 (7), pp. 1989-1995. Date of Electronic Publication: 2018 Jan 15 (Print Publication: 2018). - Publication Year :
- 2018
-
Abstract
- In mitochondria, cytochrome c oxidase (C c O) catalyses the reduction of oxygen (O <subscript>2</subscript> ) 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 C c O. A tridentate copper(ii) complex was fixed onto 5,10,15,20-tetrakis(4-sulfonatophenyl)porphinatoiron(iii) (Fe <superscript>III</superscript> TPPS) through supramolecular complexation between Fe <superscript>III</superscript> TPPS and a per- O -methylated β-cyclodextrin dimer linked by a (2,2':6',2''-terpyridyl)copper(ii) complex (Cu <superscript>II</superscript> TerpyCD <subscript>2</subscript> ). The reduced Fe <superscript>II</superscript> TPPS/Cu <superscript>I</superscript> TerpyCD <subscript>2</subscript> complex reacted with O <subscript>2</subscript> in an aqueous solution at pH 7 and 25 °C to form a superoxo-type Fe <superscript>III</superscript> -O <subscript>2</subscript> <superscript>-</superscript> /Cu <superscript>I</superscript> complex in a manner similar to C c O. The pH-dependent autoxidation of the O <subscript>2</subscript> complex suggests that water molecules gathered at the distal Cu site are possibly involved in the Fe <superscript>III</superscript> -O <subscript>2</subscript> <superscript>-</superscript> /Cu <superscript>I</superscript> superoxo complex in an aqueous solution. Electrochemical analysis using a rotating disk electrode demonstrated the role of the FeTPPS/CuTerpyCD <subscript>2</subscript> hetero-binuclear structure in the catalytic O <subscript>2</subscript> reduction reaction.
Details
- Language :
- English
- ISSN :
- 2041-6520
- Volume :
- 9
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Chemical science
- Publication Type :
- Academic Journal
- Accession number :
- 29675246
- Full Text :
- https://doi.org/10.1039/c7sc04732k