Abstract
The picosecond photodissociation of the CO and O2 forms of alpha and beta chains of hemoglobin were studied by following pi pi Soret absorption changes using a Nd3+ phosphate-glass laser, 531-nm pump pulse, 8 ps full width half maximum, and a pump-probe double-beam absorption apparatus. Three intermediates were observed within the first 50 ps after photon absorption. The most notable differences between the two monomers are the extent and rate of geminate recombination with the two ligands. We attribute this result to differences between the tertiary protein structure of the alpha and beta forms of Hb, both distal and proximal.
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