Heme proteins: quantum yield determined by the pulse method.

Abstract

We report results of the application of the "pulse method" to the study of photodissociation of various ligands from several heme proteins. By use of this technique, which allows the determination of the quantum yield of photodissociation accurately and rapidly, several ligands (CO, O(2), isocyanides) have been investigated for sperm-whale myoglobin and trout hemoglobin I. In agreement with previous results, the new data lead to the conclusion that no simple relationship exists between the quantum yield and the affinity constant in the ground state. For trout hemoglobin I, the experiments were extended to measure the quantum yield of the CO photodissociation as a function of the initial degree of saturation, from fully saturated down to the initial values of about 1.5%. The results yield additional information to that obtained by the "steady-state" method, and in particular exclude the idea that the photochemical yield is in any way dependent on the fractional saturation of the molecule with carbon monoxide.