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...
Главные авторы: | , , |
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Формат: | Journal article |
Опубликовано: |
1996
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