Linking structural dynamics and functional diversity in asymmetric catalysis

Akihiro Nojiri, Naoya Kumagai, Masakatsu Shibasaki

Research output: Contribution to journalArticlepeer-review

129 Citations (Scopus)


Proteins, the functional molecules in biological systems, are sophisticated chemical devices thathave evolved over billions of years. Their function is intimately related to their three-dimensional structure and elegantly regulated by conformational changes through allosteric regulators and a number of reversible or unidirectional post-translational modifications. This functional diversification in response to external stimuli allows for an orderly and timely progression of intra- and extracellular events. In contrast, enantioselective Catalystsc generally exhibit limited conformational flexibility and thereby exert a single specific function. Exploiting the features of conformationally flexible asymmetric ligands and the variable coordination patterns of rare earth metals, we demonstrate dynamic structural and functional changes of a catalyst in asymmetric catalysis, leading to two distinct reaction outcomes in a single flask.

Original languageEnglish
Pages (from-to)3779-3784
Number of pages6
JournalJournal of the American Chemical Society
Issue number10
Publication statusPublished - 2009 Mar 18
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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