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A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase
In mitochondria, cytochrome c oxidase (CcO) catalyses the reduction of oxygen (O(2)) 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 tridenta...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Royal Society of Chemistry
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5892347/ https://www.ncbi.nlm.nih.gov/pubmed/29675246 http://dx.doi.org/10.1039/c7sc04732k |
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author | Kitagishi, Hiroaki Shimoji, Daiki Ohta, Takehiro Kamiya, Ryo Kudo, Yasuhiro Onoda, Akira Hayashi, Takashi Weiss, Jean Wytko, Jennifer A. Kano, Koji |
author_facet | Kitagishi, Hiroaki Shimoji, Daiki Ohta, Takehiro Kamiya, Ryo Kudo, Yasuhiro Onoda, Akira Hayashi, Takashi Weiss, Jean Wytko, Jennifer A. Kano, Koji |
author_sort | Kitagishi, Hiroaki |
collection | PubMed |
description | In mitochondria, cytochrome c oxidase (CcO) catalyses the reduction of oxygen (O(2)) 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(III)TPPS) through supramolecular complexation between Fe(III)TPPS and a per-O-methylated β-cyclodextrin dimer linked by a (2,2′:6′,2′′-terpyridyl)copper(ii) complex (Cu(II)TerpyCD(2)). The reduced Fe(II)TPPS/Cu(I)TerpyCD(2) complex reacted with O(2) in an aqueous solution at pH 7 and 25 °C to form a superoxo-type Fe(III)–O(2)(–)/Cu(I) complex in a manner similar to CcO. The pH-dependent autoxidation of the O(2) complex suggests that water molecules gathered at the distal Cu site are possibly involved in the Fe(III)–O(2)(–)/Cu(I) superoxo complex in an aqueous solution. Electrochemical analysis using a rotating disk electrode demonstrated the role of the FeTPPS/CuTerpyCD(2) hetero-binuclear structure in the catalytic O(2) reduction reaction. |
format | Online Article Text |
id | pubmed-5892347 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-58923472018-04-19 A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase Kitagishi, Hiroaki Shimoji, Daiki Ohta, Takehiro Kamiya, Ryo Kudo, Yasuhiro Onoda, Akira Hayashi, Takashi Weiss, Jean Wytko, Jennifer A. Kano, Koji Chem Sci Chemistry In mitochondria, cytochrome c oxidase (CcO) catalyses the reduction of oxygen (O(2)) 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(III)TPPS) through supramolecular complexation between Fe(III)TPPS and a per-O-methylated β-cyclodextrin dimer linked by a (2,2′:6′,2′′-terpyridyl)copper(ii) complex (Cu(II)TerpyCD(2)). The reduced Fe(II)TPPS/Cu(I)TerpyCD(2) complex reacted with O(2) in an aqueous solution at pH 7 and 25 °C to form a superoxo-type Fe(III)–O(2)(–)/Cu(I) complex in a manner similar to CcO. The pH-dependent autoxidation of the O(2) complex suggests that water molecules gathered at the distal Cu site are possibly involved in the Fe(III)–O(2)(–)/Cu(I) superoxo complex in an aqueous solution. Electrochemical analysis using a rotating disk electrode demonstrated the role of the FeTPPS/CuTerpyCD(2) hetero-binuclear structure in the catalytic O(2) reduction reaction. Royal Society of Chemistry 2018-01-15 /pmc/articles/PMC5892347/ /pubmed/29675246 http://dx.doi.org/10.1039/c7sc04732k Text en This journal is © The Royal Society of Chemistry 2018 https://creativecommons.org/licenses/by/3.0/This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0) |
spellingShingle | Chemistry Kitagishi, Hiroaki Shimoji, Daiki Ohta, Takehiro Kamiya, Ryo Kudo, Yasuhiro Onoda, Akira Hayashi, Takashi Weiss, Jean Wytko, Jennifer A. Kano, Koji A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase |
title | A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase
|
title_full | A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase
|
title_fullStr | A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase
|
title_full_unstemmed | A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase
|
title_short | A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase
|
title_sort | water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5892347/ https://www.ncbi.nlm.nih.gov/pubmed/29675246 http://dx.doi.org/10.1039/c7sc04732k |
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