Measurements of the rates of CO binding to ferrous porphyrins have been used to examine two different mechanisms which have been proposed to explain protein control of heme reactivity. The results indicate that electronic control through ω-donor/acceptor interactions with the macrocyclic porphyrin ring is not important in controlling the heme reactivity of hemoglobin or of other hemoproteins. However, hydrogen bonding to the metal-bound imidazole can have a powerful influence on heme reactivity.
|Original language||English (US)|
|Number of pages||8|
|Journal||Journal of the American Chemical Society|
|State||Published - Jun 1980|
ASJC Scopus subject areas
- Colloid and Surface Chemistry