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Assignment of imidazole resonances from two‐dimensional proton NMR spectra of bovine Cu,Zn Superoxide dismutase
Author(s) -
Paci Maurizio,
Desideri Alessandro,
Sette Marco,
Ciriolo Maria R.,
Rotilio Giuseppe
Publication year - 1990
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(90)80720-4
Subject(s) - imidazole , superoxide dismutase , chemistry , spectral line , proton , proton nmr , nuclear magnetic resonance , stereochemistry , biochemistry , enzyme , physics , quantum mechanics , astronomy
Two‐dimensional 1 H‐NMR spectra were carried out on bovine Cu(I),Zn Superoxide dismutase. The ring protons of the single tyrosine and of the 4 phenylalanines were identified from COSY spectra. Prom NOESY spectra all imidazole C‐resonances could be specifically assigned to each of the 8 histidines using the crystal coordinates of the Cu(II),Zn enzyme. Since 6 histidines are involved in the structure of the active site, this result implies nearly identical active site conformations for the two oxidation states of the catalytic cycle of this enzyme, in line with its diffusion‐limited rate.