XANES of carboxy and cyanomet-myoglobin. The role of the distal histidine in the bent Fe-C-O configuration.
The ligand bonding geometry of carboxy- and cyanomet-myoglobin (MbCO and MbCN) has been measured by the XANES method (X-ray Absorption Near Edge Structure). A comparison between the ligand bonding geometry of carboxy- and cyanomet-myoglobin and of chelated protoheme methyl ester shows that the bent Fe-C-O configuration is the same in both systems. Therefore, we suggest that this configuration is not associated with any steric constraint imposed by the side chains of the aminoacid residues at the distal side of the heme pocket.
D055592:Biophysical Phenomena; D001703:Biophysics; D006418:Heme; D006420:Hemeproteins; D006639:Histidine; D008786:Metmyoglobin / Q000031:analogs & derivatives; D009211:Myoglobin; D011487:Protein Conformation; D013057:Spectrum Analysis; D014965:X-Rays
D006420:Hemeproteins; D009211:Myoglobin; C018013:carboxymyoglobin; C007177:cyanometmyoglobin; D008786:Metmyoglobin; D006418:Heme; D006639:Histidine