Autoxidation of hemoglobin enhanced by dissociation into dimers.
Autoxidation as a function of hemoglobin concentration indicates a 17-fold increase in the rate of autoxidation from 0.25 (%/h) to 4.3 (%/h) when tetrameric oxyhemoglobin dissociates into dimers. As a result of this large enhancement, a contribution of dissociation to the autoxidation is evident even at relatively high concentrations of hemoglobin for which it is usually considered that dissociation can be neglected. The mechanism for this phenomenon is attributed to alterations in the ligand pocket which occur when constraints due to subunit contacts within the R-state are eliminated.
Zhang
L
L
Laboratory of Cellular and Molecular Biology, National Institutes of Health, National Institute on Aging, Baltimore, Maryland 21224.
Levy
A
A
Rifkind
J M
JM
D004912:Erythrocytes / Q000378:metabolism; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D010084:Oxidation-Reduction
D006454:Hemoglobins