A Redetermination of the Crystal and Molecular Structure of Glutathione (gamma-L-Glutamyl-L-cysteinylglycine) at 120 K.

Publisher Website
Google Scholar
Abstract
The crystal and molecular structure of the tripeptide .gamma.-L-glutamyl-L-cysteinylglycine (glutathione) has been redetermined at 120 K using 1628 reflections with 1 > 2.5 .sigma.I. The unit cell is orthorhombic, P212121, with cell dimensions a = 5.622 (2), b = 8.781(3), c = 28.023 (10) .ANG.. The final R-factor was 0.056. The overall molecular geometry agrees with the first structure determination, but several large differences in bond lengths and bond angles are pointed out. The SH group is involved in a weak hydrogen bond. A very short intermolecular contact occurs between the C-terminal carboxylic group and the carbonyl group in the .gamma.-glutamyl peptide bond (C .cntdot..cntdot..cntdot. O 2.86 .ANG.),accompanied by a substantial deviation from planarity for the peptide unit (.omega.1 = -167.0.degree.).

This publication has 2 references indexed in Scilit: