(1) Dipartimento di Fisica and Istituto Nazionale di Fisica della Materia, Universita' “La Sapienza”, I-00185 Roma, Italy, IT;(2) Dipartimento di Medicina Sperimentale, Universita' dell'Aquila, I-67100 L'Aquila, Italy, IT
Abstract:
We present the results of a comparative study of the binding of carbon monoxide to myoglobin in glycerol/buffer solution with different concentrations of guanidine hydrochloride, under extended illumination over the temperature range 30 – 80 K. The changes in the Soret band indicate that the folding state of the protein is a key parameter in determining the photodissociation process and the relaxation rate of the protein. Received: 30 January 1997 / Accepted: 14 August 1997