| pubmed-article:15772162 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15772162 | lifeskim:mentions | umls-concept:C0039421 | lld:lifeskim |
| pubmed-article:15772162 | lifeskim:mentions | umls-concept:C0020286 | lld:lifeskim |
| pubmed-article:15772162 | lifeskim:mentions | umls-concept:C0022634 | lld:lifeskim |
| pubmed-article:15772162 | lifeskim:mentions | umls-concept:C0596918 | lld:lifeskim |
| pubmed-article:15772162 | lifeskim:mentions | umls-concept:C1705822 | lld:lifeskim |
| pubmed-article:15772162 | lifeskim:mentions | umls-concept:C0301630 | lld:lifeskim |
| pubmed-article:15772162 | lifeskim:mentions | umls-concept:C0348011 | lld:lifeskim |
| pubmed-article:15772162 | lifeskim:mentions | umls-concept:C1705938 | lld:lifeskim |
| pubmed-article:15772162 | lifeskim:mentions | umls-concept:C2004457 | lld:lifeskim |
| pubmed-article:15772162 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:15772162 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:15772162 | pubmed:dateCreated | 2005-3-30 | lld:pubmed |
| pubmed-article:15772162 | 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. | lld:pubmed |
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| pubmed-article:15772162 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15772162 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15772162 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15772162 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:15772162 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:15772162 | pubmed:author | pubmed-author:WardThomas... | lld:pubmed |
| pubmed-article:15772162 | pubmed:author | pubmed-author:HumbertNicola... | lld:pubmed |
| pubmed-article:15772162 | pubmed:author | pubmed-author:LetondorChris... | lld:pubmed |
| pubmed-article:15772162 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15772162 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:15772162 | pubmed:volume | 102 | lld:pubmed |
| pubmed-article:15772162 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15772162 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15772162 | pubmed:pagination | 4683-7 | lld:pubmed |
| pubmed-article:15772162 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15772162 | pubmed:meshHeading | pubmed-meshheading:15772162... | lld:pubmed |
| pubmed-article:15772162 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15772162 | pubmed:articleTitle | Artificial metalloenzymes based on biotin-avidin technology for the enantioselective reduction of ketones by transfer hydrogenation. | lld:pubmed |
| pubmed-article:15772162 | pubmed:affiliation | Institute of Chemistry, University of Neuchâtel, Avenue Bellevaux 51, CP 2, CH-2007 Neuchâtel, Switzerland. | lld:pubmed |
| pubmed-article:15772162 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15772162 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15772162 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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