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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Bibliographische Detailangaben
Veröffentlicht in:	Chemical communications (Cambridge, England) England), 2008-04 (14), p.1665-1667
Hauptverfasser:	Zhang, Jun-Long, Garner, Dewain K, Liang, Lei, Chen, Qian, Lu, Yi
Format:	Artikel
Sprache:	eng
Schlagworte:	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
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Beschreibung
Zusammenfassung:	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.
ISSN:	1359-7345 1364-548X 1364-548X
DOI:	10.1039/b718915j