Crown ether-mediated extraction and functional conversion of cytochrome C in ionic liquids.
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.
Shimojo
Kojiro
K
Division of Environment and Radiation Sciences, Nuclear Science and Energy Directorate, Japan Atomic Energy Agency, Tokai-mura, Ibaraki 319-1195, Japan.
Nakashima
Kazunori
K
Kamiya
Noriho
N
Goto
Masahiro
M
D000818:Animals; D043844:Crown Ethers; D045304:Cytochromes c / Q000737:chemistry* / Q000378:metabolism*; D006736:Horses; D007477:Ions / Q000737:chemistry; D015394:Molecular Structure; D010544:Peroxidases / Q000737:chemistry / Q000378:metabolism
D043844:Crown Ethers; D007477:Ions; D045304:Cytochromes c; D010544:Peroxidases