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Excitation of HbCO by a single 6-psec 530-nm pulse results in photodissociation with a first-order constant of 0.89 X 10(11) sec-1. The kinetics of photodissociation, monitored by following absorbance changes in the Soret band at 440 nm, are interpreted as corresponding to predissociation followed by a corssing into a dissociative state. Subsequent recombination of CO with the porphyrin system and protein structural transformations were monitored by use of a continuous He-Cd laser beam spatially coincident with the photolysis and Soret interrogation beams at the sample. We find that the latter events take place in three distinct time regions, depending on exciation pulse energy and repetition rate. Exictation of HbCO with a single pulse (0.8--5 mJ) results in a relaxation to the ground state with an associative first-order constant of 5 X 10(3) sec-1. With a 100-pulse train (approximately 7.5 mJ), a new decay grows with a rate constant of 63 sec-1. For a pulse-train energy of 12 mJ or higher, a delay occurs at the onset of the second (slower) recombination.

Picosecond photodissociation and subsequent recombination processes in carbon monoxide hemoglobin.