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Catalytic Hydrolysis of Peptides by Cerium( IV )
Author(s) -
Takarada Tohru,
Yashiro Morio,
Komiyama Makoto
Publication year - 2000
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/1521-3765(20001103)6:21<3906::aid-chem3906>3.0.co;2-j
Subject(s) - chemistry , hydrolysis , tripeptide , amide , catalysis , medicinal chemistry , cerium , peptide , peptide bond , stereochemistry , organic chemistry , biochemistry
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 3.5×10 −1 and 2.8×10 −1 h −1 , with [Ce(NH 4 ) 2 (NO 3 ) 6 ] 0 =10 m M (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 1 H NMR spectroscopy. The Ce IV ion is therefore one of the most active catalysts for peptide hydrolysis.