title: Protein conformation-induced modulation of ligand binding kinetics: a femtosecond mid-IR study of nitric oxide binding trajectories in myoglobin.
abstract: By directly probing the photolyzed NO from MbNO at physiological conditions, the rebinding trajectories of the photoproduct were obtained, from which we found that a time-dependent barrier arising from protein relaxation on the same time scale as that of the rebinding process is responsible for the NO nonexponential rebinding.
authors.affiliation: Department of Chemistry, Pusan National University, Busan 609-735, Korea.
authors.forename: Seongheun
authors.initials: S
authors.lastname: Kim
authors.forename: Manho
authors.initials: M
authors.lastname: Lim
mesh_terms: D007700:Kinetics; D008024:Ligands; D009211:Myoglobin / Q000737:chemistry*; D009569:Nitric Oxide / Q000737:chemistry*; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared / Q000379:methods; D013997:Time Factors
chemical_list: D008024:Ligands; D009211:Myoglobin; D009569:Nitric Oxide