Protein conformation-induced modulation of ligand binding kinetics: a femtosecond mid-IR study of nitric oxide binding trajectories in myoglobin

Seongheun Kim; Manho Lim

doi:10.1021/ja0502270

Protein conformation-induced modulation of ligand binding kinetics: a femtosecond mid-IR study of nitric oxide binding trajectories in myoglobin

J Am Chem Soc. 2005 Jun 29;127(25):8908-9. doi: 10.1021/ja0502270.

Authors

Seongheun Kim¹, Manho Lim

Affiliation

¹ Department of Chemistry, Pusan National University, Busan 609-735, Korea.

PMID: 15969541
DOI: 10.1021/ja0502270

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Kinetics
Ligands
Myoglobin / chemistry*
Nitric Oxide / chemistry*
Protein Conformation
Spectrophotometry, Infrared / methods
Time Factors

Substances

Ligands
Myoglobin
Nitric Oxide