Structural interpretation of low-temperature heme-ligand recombination rates in myoglobin.
The nonexponential recombination of photodissociated heme-CO and heme-O2 in myoglobin, which is geminate at T less than 180 K, is interpreted as being due to a narrow, random distribution of ligand transfer distances in the heme pocket. This permits evaluation of the most probable recombination rate which is shown to be consistent with ligand tunneling.
D006418:Heme; D007700:Kinetics; D008433:Mathematics; D008956:Models, Chemical; D009211:Myoglobin; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013696:Temperature
D009211:Myoglobin; D006418:Heme