Article
Origin of the pH-dependent spectroscopic properties of pentacoordinate metmyoglobin variants.
Biochemistry - 22 Aug 1995
Bogumil R, Maurus R, Hildebrand D P, Brayer G D, Mauk A G
Abstract excerpt
The pH dependence of the electronic and EPR spectra of two variants of horse heart myoglobin (Mb) in which the distal His64 ligand has been replaced by either Thr or Ile has been studied. Both of these variants exhibit spectroscopic changes with pH that are indicative of a transition between two...
Topics
- Animals
- Buffers
- Electron Spin Resonance Spectroscopy
- Histidine
- Horses
- Hydrogen-Ion Concentration
- Isoleucine
- Metmyoglobin
- Mutation
- Myocardium
- Protein Conformation
- Spectrum Analysis
- Threonine
