Solvent composition and viscosity effects on the kinetics of CO binding to horse myoglobin.

@article{Kleinert1998SolventCA,
  title={Solvent composition and viscosity effects on the kinetics of CO binding to horse myoglobin.},
  author={T. Kleinert and Wolfgang Doster and H. M. Ottoline Leyser and Winfried Petry and Volker Schwarz and Marcus Settles},
  journal={Biochemistry},
  year={1998},
  volume={37 2},
  pages={717-33}
}
Ligand binding to myoglobin in aqueous solution involves two kinetic components, one extramolecular and one intramolecular, which have been interpreted in terms of two sequential kinetic barriers. In mixed solvents and sub-zero temperatures, the outer barrier increases and the inner barrier splits into several components, giving rise to fast intramolecular recombination. The nature of these barriers and their relation to structural relaxation are examined using the effect of solvent composition… CONTINUE READING