Catalytic hydrolysis of peptides by cerium(IV)

Tohru Takarada, Morio Yashiro, Makoto Komiyama

研究成果: ジャーナルへの寄稿学術誌査読

67 被引用数 (Scopus)

抄録

Oligopeptides are efficiently hydrolyzed by Ce(IV) to the corresponding amino acids under mild conditions. The pseudo first-order rate constants for the hydrolysis of H-Gly-Phe-OH and H-Gly-Gly-OH at pH 7.0 and 50°C are 3.5 x 10-1 and 2.8 x 10-1h-1, with [Ce(NH4)2(NO3)6]0=10mM (the half-lives are 2.0 and 2.5 h). The catalytic activity of the Ce(IV) is far greater than those of other lanthanide ions and non-lanthanide ions. No oxidative cleavage was observed under the reaction conditions. Catalytic turnover of the Ce(IV) was also evidenced. The hydrolysis is fast especially when the substrates have no metal-coordinating side chains. Tripeptides and tetrapeptides are hydrolyzed at the similar rates as the dipeptides. In the hydrolysis of tripeptides, the amide linkage near the N-terminus is preferentially hydrolyzed. Neither the N-carbobenzyloxy derivative nor the amide of H-Gly-Phe-OH is hydrolyzed to a measurable extent, showing that both the terminal amino group and the carboxylate are coordinated to the Ce(IV) ion. This complexation is further confirmed by 1H NMR spectroscopy. The Ce(IV) ion is therefore one of the most active catalysts for peptide hydrolysis.

本文言語英語
ページ(範囲)3906-3913
ページ数8
ジャーナルChemistry - A European Journal
6
21
DOI
出版ステータス出版済み - 11月 3 2000
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 化学 (全般)

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