Article
Mutational effects on the spectroscopic properties and biological activities of oxidized bovine adrenodoxin, and their structural implications.
European journal of biochemistry - 1 Jul 1995
Beckert V, Schrauber H, Bernhardt R, Van Dijk A A, Kakoschke C, Wray V
Abstract excerpt
Of the aromatic 1H-NMR signals of oxidized bovine adrenodoxin only those of His56 showed intrinsic chemical shift changes upon replacement of Tyr82 by Ser or Leu, that must arise from a loss of a through-space ring-current effect of the tyrosine ring in these mutants. Thus, of the three His residues contained in adrenodoxin, His56 is closest to Tyr82, and hence to the highly acidic determinant region of...
Topics
- Adrenodoxin
- Amides
- Amino Acid Sequence
- Animals
- Cattle
- Electron Spin Resonance Spectroscopy
- Hydrogen-Ion Concentration
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation