Premium
X‐band ESEEM spectroscopy of 15 N substituted native and inhibitor‐bound superoxide dismutase
Author(s) -
Dikanov Sergei,
Felli Isabella,
Viezzoli Maria-Silvia,
Spoyalov Andrei,
Hüttermann Jürgen
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00406-4
Subject(s) - superoxide dismutase , chemistry , spectroscopy , biochemistry , enzyme , physics , quantum mechanics
The hyperfine couplings of the remote nitrogens of histidine ligands are determined for the first time by an X‐band ESEEM spectroscopy study of 15 N‐substituted superoxide dismutase (SOD). They show a significant difference between two groups of ligands with different orientation relative to the metal ion. The ESEEM spectra of 15 N SOD with cyanide as an inhibitor containing 14 N and 15 N are also discussed. They allow some conclusions to be drawn about structural changes upon inhibitor binding and indicate the necessity of further multifrequency investigations.