Crown ether-mediated extraction and functional conversion of cytochrome c in ionic liquids

Kojiro Shimojo; Kazunori Nakashima; Noriho Kamiya; Masahiro Goto

doi:10.1021/bm050847t

Crown ether-mediated extraction and functional conversion of cytochrome c in ionic liquids

Kojiro Shimojo, Kazunori Nakashima, Noriho Kamiya, Masahiro Goto

Applied Chemistry

Research output: Contribution to journal › Article › peer-review

112 Citations (Scopus)

Abstract

We report that a macrocyclic ligand enables transfer of a protein from an aqueous phase to ionic liquids. The extraction behavior of heme protein cytochrome c (Cyt-c) from an aqueous phase into ionic liquids was investigated with crown ethers. A hydroxyl-group-containing ionic liquid with dicyclohexano-18-crown-6 was found to be capable of quantitative partitioning of Cyt-c, whereas the protein transfer using conventional organic solvents was negligibly small. Furthermore, we clarified that Cyt-c solubilized in ionic liquids caused a structural transformation of Cyt-c, which triggers its functional conversion from an electron-transfer protein to peroxidase.

Original language	English
Pages (from-to)	2-5
Number of pages	4
Journal	Biomacromolecules
Volume	7
Issue number	1
DOIs	https://doi.org/10.1021/bm050847t
Publication status	Published - Jan 2006

All Science Journal Classification (ASJC) codes

Bioengineering
Biomaterials
Polymers and Plastics
Materials Chemistry

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10.1021/bm050847t

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abstract = "We report that a macrocyclic ligand enables transfer of a protein from an aqueous phase to ionic liquids. The extraction behavior of heme protein cytochrome c (Cyt-c) from an aqueous phase into ionic liquids was investigated with crown ethers. A hydroxyl-group-containing ionic liquid with dicyclohexano-18-crown-6 was found to be capable of quantitative partitioning of Cyt-c, whereas the protein transfer using conventional organic solvents was negligibly small. Furthermore, we clarified that Cyt-c solubilized in ionic liquids caused a structural transformation of Cyt-c, which triggers its functional conversion from an electron-transfer protein to peroxidase.",

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AB - We report that a macrocyclic ligand enables transfer of a protein from an aqueous phase to ionic liquids. The extraction behavior of heme protein cytochrome c (Cyt-c) from an aqueous phase into ionic liquids was investigated with crown ethers. A hydroxyl-group-containing ionic liquid with dicyclohexano-18-crown-6 was found to be capable of quantitative partitioning of Cyt-c, whereas the protein transfer using conventional organic solvents was negligibly small. Furthermore, we clarified that Cyt-c solubilized in ionic liquids caused a structural transformation of Cyt-c, which triggers its functional conversion from an electron-transfer protein to peroxidase.

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Crown ether-mediated extraction and functional conversion of cytochrome c in ionic liquids

Abstract

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