The kinetics of ligand binding for diverse mammalian myoglobins and the effects of substitutions outside the heme cavity.
1. We report rate constants for oxygen dissociation and for oxygen, carbon monoxide, azide, and cyanide binding to whale, horse, dog, beef and human myoglobins. 2. For azide binding, rate constants can vary by at least a factor of two for substitutions outside the heme cavity. Azide binding may be affected by a substitution at residue 66 in the E helix, a site suggested by Case & Karplus (1979) J. molec. Biol. 132, 343-368, to be on a reactive path to the heme. 3. The oxygen and CO data show that substitutions outside the heme cavity can affect rate constants by at least a factor of 1.5. 4. The oxygen equilibrium constant was correlated with the metabolite rate of the corresponding species, in accord with the Wyman (1966) J. biol. Chem. 241, 115-121, model for facilitated diffusion of oxygen.
D000818:Animals; D001386:Azides / Q000378:metabolism*; D002248:Carbon Monoxide / Q000378:metabolism; D002417:Cattle; D003486:Cyanides / Q000378:metabolism*; D004285:Dogs; D006736:Horses; D006801:Humans; D007700:Kinetics; D008024:Ligands / Q000378:metabolism; D009211:Myoglobin / Q000378:metabolism*; D010101:Oxygen Consumption; D013045:Species Specificity; D014907:Whales
D001386:Azides; D003486:Cyanides; D008024:Ligands; D009211:Myoglobin; D002248:Carbon Monoxide