1. 1. The rate constants and ΔH° for the non-cooperative dimeric Busycon myoglobin are: oxygen, k' = 4.75 × 107M-1, k = 71 sec-1, and CO, l′ -3.46 × 105 M-li]1sec-1, l = 0.0052 sec-1 at 20°C, pH 7. ΔH° = -3 kcal/mol for O2 and CO. 2. Log-log plots of k vs K for oxygen and of l′ vs L for CO binding for numerous non-cooperative hemoglobins and myoglobins point to a large steric influence of the protein on heme ligation reactions. Many of the proteins behave as "R" state for one ligand, but "T" for the other.
|Original language||English (US)|
|Number of pages||7|
|Journal||Comparative Biochemistry and Physiology -- Part A: Physiology|
|State||Published - 1984|
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