Protein conformation-induced modulation of ligand binding kinetics: a femtosecond mid-IR study of nitric oxide binding trajectories in myoglobin.
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.
Kim
Seongheun
S
Department of Chemistry, Pusan National University, Busan 609-735, Korea.
Lim
Manho
M
D007700:Kinetics; D008024:Ligands; D009211:Myoglobin / Q000737:chemistry*; D009569:Nitric Oxide / Q000737:chemistry*; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared / Q000379:methods; D013997:Time Factors
D008024:Ligands; D009211:Myoglobin; D009569:Nitric Oxide