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.
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Received: 30 January 1997 / Accepted: 14 August 1997
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Natali, F., Moretti, L., Boffi, F. et al. Light induced states in MbCO denatured with Guanidine hydrochloride. Eur Biophys J 27, 1–7 (1998). https://doi.org/10.1007/s002490050104
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DOI: https://doi.org/10.1007/s002490050104