Protein scaffold of a designed metalloenzyme enhances the chemoselectivity in sulfoxidation of thioanisole
We demonstrate that incorporation of MnSalen into a protein scaffold enhances the chemoselectivity in sulfoxidation of thioanisole and find that both the polarity and hydrogen bonding of the protein scaffold play an important role in tuning the chemoselectivity.
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Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2008-04 (14), p.1665-1667 |
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creator | Zhang, Jun-Long Garner, Dewain K Liang, Lei Chen, Qian Lu, Yi |
description | We demonstrate that incorporation of MnSalen into a protein scaffold enhances the chemoselectivity in sulfoxidation of thioanisole and find that both the polarity and hydrogen bonding of the protein scaffold play an important role in tuning the chemoselectivity. |
doi_str_mv | 10.1039/b718915j |
format | Article |
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subjects | Chelating Agents - chemistry chemical compounds chemical reactions chemoselectivity Coenzymes - chemistry Computer Simulation Ethylenediamines - chemistry Hydrogen Bonding Manganese - chemistry Metalloproteases - chemistry Models, Molecular Molecular Structure Organometallic Compounds - chemical synthesis Organometallic Compounds - chemistry Protein Engineering scaffolding proteins Substrate Specificity Sulfides - chemistry Sulfoxides - chemistry |
title | Protein scaffold of a designed metalloenzyme enhances the chemoselectivity in sulfoxidation of thioanisole |
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