Oxygen binding in cyanmet hybrid and normal hemoglobins: applicability of sequential and two-state concerted models.
The cyanmet hybrid hemoglobins alpha(2)beta(+CN)(2) and alpha(+CN)(2)beta(2) are widely held to be similar or equivalent in structure and subunit interactions to the partially oxygen-liganded species alpha(2)(beta * O(2))(2) and (alpha * O(2))(2)beta(2), respectively. An analysis of precise data on oxygen binding to the cyanmet hybrids and normal hemoglobin shows that if this is the case, then cooperative ligand binding in hemoglobin is more properly described by some model of the sequential type than by any twostate concerted model.
D001665:Binding Sites; D006454:Hemoglobins; D006801:Humans; D007700:Kinetics; D008024:Ligands; D008706:Methemoglobin; D008956:Models, Chemical; D009570:Nitriles; D010108:Oxyhemoglobins
D006454:Hemoglobins; D008024:Ligands; D009570:Nitriles; D010108:Oxyhemoglobins; D008706:Methemoglobin