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pubmed-article:16323831pubmed:abstractText[structure: see text] Molecular clips functionalized by phosphonate or phosphate groups bind thiamine diphosphate (TPP) and S-adenosylmethionine (SAM) with high affinity in water; both sulfur-based cofactors transfer organic groups to biomolecules. For TPP, various analytical tools point toward a simultaneous insertion of both heterocyclic rings into the electron-rich clip cavity. Similarly, SAM is also embedded with its sulfonium moiety inside the receptor cavity. This paves the way for enzyme models and direct interference with enzymatic processes.lld:pubmed
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pubmed-article:16323831pubmed:pagination10227-37lld:pubmed
pubmed-article:16323831pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:16323831pubmed:year2005lld:pubmed
pubmed-article:16323831pubmed:articleTitleInclusion of thiamine diphosphate and S-adenosylmethionine at their chemically active sites.lld:pubmed
pubmed-article:16323831pubmed:affiliationDepartment of Chemistry, University of Marburg, Hans-Meerwein-Strasse, 35032 Marburg, Germany. schradet@staff.uni-marburg.delld:pubmed
pubmed-article:16323831pubmed:publicationTypeJournal Articlelld:pubmed
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