Control of myoglobin electron-transfer rates by the distal (nonbound) histidine residue
Changing the distal histidine (H64) of sperm-whale myoglobin into any of the following residues-valine, leucine, methionine, glycine, or phenylalanine-causes a dramatic improvement in the reversibility (electron-transfer kinetics) and reproducibility of the direct electrochemistry. Cyclic voltammogr...
| Main Authors: | , , |
|---|---|
| Format: | Journal article |
| Published: |
1996
|