Linked Life Data

13129333

Source:http://linkedlifedata.com/resource/pubmed/id/13129333

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
38
pubmed:dateCreated
2003-9-17
pubmed:abstractText
Supramolecular complexation with 18-crown-6 significantly converted catalytically inactive cytochrome c (biological form) to catalytically active synzyme (artificial form). Although a family of cytochrome c proteins does not work as enzymes in nature, crown ether complexation modified their heme coordination structures and functionally activated them to promote the asymmetric oxidation of racemic sulfoxides at low temperature. Horse heart, pigeon breast, and yeast cytochrome c proteins were demonstrated to form supramolecular complexes with 18-crown-6 in methanol, which effectively oxidized (S)-isomers of naphthyl methyl sulfoxide, methyl tolyl sulfoxide, isopropyl phenyl sulfoxide, benzyl methyl sulfoxide, and 4-methylsulfenyl acetophenone at -40 degrees C. Because horse heart and pigeon breast cytochromes c exhibited more efficient and higher enantiomer-selective activities than yeast cytochrome c, a proper combination of cytochrome c and crown ether offers a new class of cold-active synzymes promoting nonbiological asymmetric oxidation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11478-9
pubmed:dateRevised
2008-1-17
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Chemical activation of cytochrome c proteins via crown ether complexation: cold-active synzymes for enantiomer-selective sulfoxide oxidation in methanol.
pubmed:affiliation
Department of Chemistry, Graduate School of Science, Osaka City University, Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't