Kinetic properties of cobalt--iron hybrid hemoglobins.
The replacement of O2 with CO was studied on cobalt-iron hemoglobin hybrids. Both proto- and mesocobalt hemes were used for the reconstitution. In the oxy quaternary conformation no difference is observed between alpha- and beta-subunits when only proto hemes are present in the hybrid (k4 = 30 s-1, k'4/l'4 = 2.5). If Co-meso heme is present on the beta-chains the binding properties of the partner subunit are modified (k'4/l'4 = 4).
D002248:Carbon Monoxide / Q000378:metabolism; D006454:Hemoglobins / Q000378:metabolism*; D007501:Iron / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D010100:Oxygen / Q000378:metabolism; D011487:Protein Conformation; D055503:Protein Multimerization
D006454:Hemoglobins; D046911:Macromolecular Substances; C007098:coboglobin; D002248:Carbon Monoxide; D007501:Iron; D010100:Oxygen