title: Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O.
abstract: The relative orientations of carbon monoxide (CO) bound to and photodissociated from myoglobin in solution have been determined with time-resolved infrared polarization spectroscopy. The bound CO is oriented < or = 7 degrees from the heme normal, corresponding to nearly linear FE-C-O. Upon dissociation from the Fe, CO becomes trapped in a docking site that orientationally constrains it to lie approximately in the plane of the heme. Because the bound and "docked" CO are oriented in nearly orthogonal directions CO binding from the docking site is suppressed. These solutions results help to establish how myoglobin discriminates against CO, a controversial issue dominated by the misconception that Fe-C-O is bent.
authors.affiliation: Department of Chemistry, Harvard University, Cambridge, MA 02138 USA.
authors.forename: M
authors.initials: M
authors.lastname: Lim
authors.forename: T A
authors.initials: TA
authors.lastname: Jackson
authors.forename: P A
authors.initials: PA
authors.lastname: Anfinrud
mesh_terms: D001665:Binding Sites; D002248:Carbon Monoxide / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D008024:Ligands; D008027:Light; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism; D010100:Oxygen / Q000737:chemistry / Q000378:metabolism; D010782:Photolysis; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D013696:Temperature
chemical_list: D008024:Ligands; D009211:Myoglobin; D002248:Carbon Monoxide; D010100:Oxygen