Resonance Raman spectroscopy reveals novel ligation properties of the porcine myoglobin double mutant H64V/V68H.
A resonance Raman spectroscopic study of the porcine myoglobin double mutant H64V/V68H has confirmed that the ferric form is bis-histidine ligated, has revealed that the bis-histidine ligation is retained on reduction to the ferrous form, and has demonstrated that CO can displace the ligated distal histidine to produce a ferrous CO form which has a low steady-state photolability, indicating that the replacement histidine blocks the CO escape route from the binding site.
D000818:Animals; D001665:Binding Sites; D002248:Carbon Monoxide / Q000378:metabolism; D006639:Histidine / Q000737:chemistry* / Q000378:metabolism*; D007501:Iron / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D009211:Myoglobin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015202:Protein Engineering; D013053:Spectrophotometry; D013059:Spectrum Analysis, Raman; D013552:Swine
D009211:Myoglobin; C018013:carboxymyoglobin; D006639:Histidine; D002248:Carbon Monoxide; D007501:Iron