Article
Structural and spectroscopic studies of azide complexes of horse heart myoglobin and the His-64-->Thr variant.
The Biochemical journal - 15 May 1998
Maurus R, Bogumil R, Nguyen N T, Mauk A G, Brayer G
Abstract excerpt
The high-resolution X-ray crystallographic structures of horse heart azidometmyoglobin complexes of the wild-type protein and the His-64-->Thr variant have been determined to 2.0 and 1.8 A respectively. Azide binds to wild-type metmyoglobin in a bent configuration with an Fe-N-1-N-3 angle of 119...
Topics
- Animals
- Azides
- Crystallography, X-Ray
- Electron Spin Resonance Spectroscopy
- Heme
- Horses
- Hydrogen Bonding
- Models, Molecular
- Molecular Conformation
- Molecular Sequence Data
- Mutation
- Myocardium
- Myoglobin
- Spectroscopy, Fourier Transform Infrared