Explaining the highly enantiomeric photocyclodimerization of 2-anthracenecarboxylate bound to human serum albumin using time-resolved anisotropy studies

Denis Fuentealba, Hanako Kato, Masaki Nishijima, Gaku Fukuhara, Tadashi Mori, Yoshihisa Inoue, Cornelia Bohne

研究成果: Article査読

48 被引用数 (Scopus)

抄録

The mechanism for the high enantiomeric excess (ee) (80-90%) observed in the photocyclodimerization of 2-anthracenecarboxylate (AC) in the chiral binding sites of human serum albumin (HSA) was studied using fluorescence anisotropy. A long rotational correlation time of 36 ns was observed for the excited states of the ACs bound to the HSA site responsible for the high ee, suggesting that the ACs have restricted rotational mobility in this site. The ACs in this site have the same prochiral face protected by the protein, and this protection is responsible for the high ee observed. These insights provide a strategy for the rational design of supramolecular photochirogenic systems.

本文言語English
ページ(範囲)203-209
ページ数7
ジャーナルJournal of the American Chemical Society
135
1
DOI
出版ステータスPublished - 2013 1 9
外部発表はい

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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