We present the results of a comparative study of the binding of carbon
monoxide to myoglobin in glycerol/buffer solution with different conc
entrations of guanidine hydrochloride, under extended illumination ove
r the temperature range 30-80 K. The changes in the Sorer band indicat
e that the folding state of the protein is a key parameter in determin
ing the photodissociation process and the relaxation rate of the prote
in.