Protein response to photodissociation of CO from carbonmonoxymyoglobin probed by time-resolved infrared spectroscopy of the amide I band

Time-resolved infrared spectroscopy (TRIR) was used to examine alterations in protein conformations combined with carbon monoxide's ligation interactions, in myoglobin (Mb). Alterations in the secondary structure of proteins connected with the global easing of the protein helices after photodissociation of CO are reasons for TRIR variation characteristics of Mb.