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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
2005-3-30
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pubmed:abstractText |
Most physiological and biotechnological processes rely on molecular recognition between chiral (handed) molecules. Manmade homogeneous catalysts and enzymes offer complementary means for producing enantiopure (single-handed) compounds. As the subtle details that govern chiral discrimination are difficult to predict, improving the performance of such catalysts often relies on trial-and-error procedures. Homogeneous catalysts are optimized by chemical modification of the chiral environment around the metal center. Enzymes can be improved by modification of gene encoding the protein. Incorporation of a biotinylated organometallic catalyst into a host protein (avidin or streptavidin) affords versatile artificial metalloenzymes for the reduction of ketones by transfer hydrogenation. The boric acid.formate mixture was identified as a hydrogen source compatible with these artificial metalloenzymes. A combined chemo-genetic procedure allows us to optimize the activity and selectivity of these hybrid catalysts: up to 94% (R) enantiomeric excess for the reduction of p-methylacetophenone. These artificial metalloenzymes display features reminiscent of both homogeneous catalysts and enzymes.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-10021402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-10082986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-11710063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-11738181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-12670237,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-12790539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-12837091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-12914497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-15062771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-15079053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-15106972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-15227530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-15255712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-15339144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-15369356,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-15521760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-15624156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15772162-8874057
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
102
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4683-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15772162-Biotin,
pubmed-meshheading:15772162-Boric Acids,
pubmed-meshheading:15772162-Catalysis,
pubmed-meshheading:15772162-Chemical Engineering,
pubmed-meshheading:15772162-Formic Acids,
pubmed-meshheading:15772162-Hydrogenation,
pubmed-meshheading:15772162-Ketones,
pubmed-meshheading:15772162-Ligands,
pubmed-meshheading:15772162-Metalloproteases,
pubmed-meshheading:15772162-Models, Chemical,
pubmed-meshheading:15772162-Oxidation-Reduction,
pubmed-meshheading:15772162-Stereoisomerism,
pubmed-meshheading:15772162-Streptavidin
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pubmed:year |
2005
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pubmed:articleTitle |
Artificial metalloenzymes based on biotin-avidin technology for the enantioselective reduction of ketones by transfer hydrogenation.
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pubmed:affiliation |
Institute of Chemistry, University of Neuchâtel, Avenue Bellevaux 51, CP 2, CH-2007 Neuchâtel, Switzerland.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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