Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins.
Ligand-binding kinetics of native and reconstituted sperm-whale myoglobin were studied in relation to haem orientational disorder by rapid kinetic methods. In addition, native yellow-fin-tuna myoglobin with significant amount of haem disorder was also used. The O2 dissociation and association rates were found for the proteins with different degrees of haem disorder, and these results suggest that the isomers are characterized by almost identical kinetic parameters. Rates of CO recombination after photolysis were also identical for the two orientational isomers. The results clearly indicate that the rotation of the haem about the alpha-gamma meso axis has little or no effect on the ligand-binding properties of these myoglobins.
D000818:Animals; D002248:Carbon Monoxide / Q000378:metabolism; D002591:Cetacea / Q000378:metabolism*; D005399:Fishes / Q000378:metabolism*; D006418:Heme; D007700:Kinetics; D008024:Ligands; D009211:Myoglobin / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism; D010782:Photolysis; D011485:Protein Binding; D011487:Protein Conformation; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D014413:Tuna / Q000378:metabolism*; D014907:Whales / Q000378:metabolism*
D008024:Ligands; D009211:Myoglobin; D006418:Heme; D002248:Carbon Monoxide; D010100:Oxygen