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
Hauptverfasser: Zhang, Jun-Long, Garner, Dewain K, Liang, Lei, Chen, Qian, Lu, Yi
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container_issue 14
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container_title Chemical communications (Cambridge, England)
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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
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source MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection
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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