X‐band ESEEM spectroscopy of 15N substituted native and inhibitor‐bound superoxide dismutase

FEBS Letters

Viezzoli, Maria-Silvia¹  Dikanov, Sergei²  Felli, Isabella¹  Hüttermann, Jürgen²  Spoyalov, Andrei³ 

[1] Department of Chemistry, University of Florence, Via G. Capponi 7, 50121 Florence, Italy;Fachrichtung Biophysik und Physikalische Grundlagen der Medizin, Universität des Saarlandes, Klinikum Bau 76, 66421 Homburg Saar, Germany;Institute of Chemical Kinetics and Combustion, Russian Academy of Sciences, Novosibirsk 630090, Russian Federation

关键词: Superoxide dismutase (SOD);    Electron spin echo envelope modulation (ESEEM) spectroscopy;    Histidine residue;    Remote nitrogen;    Hyperfine coupling;   

DOI  :  10.1016/0014-5793(94)00406-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The hyperfine couplings of the remote nitrogens of histidine ligands are determined for the first time by an X-band ESEEM spectroscopy study of ¹⁵N-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 ¹⁵N SOD with cyanide as an inhibitor containing ¹⁴N and ¹⁵N are also discussed. They allow some conclusions to be drawn about structural changes upon inhibitor binding and indicate the necessity of further multifrequency investigations.

【 授权许可】

Unknown