Structural interpretation of low-temperature heme-ligand recombination rates in myoglobin

FEBS Lett. 1985 Apr 22;183(2):191-4.

Abstract

The nonexponential recombination of photodissociated heme-CO and heme-O2 in myoglobin, which is geminate at T less than 180 K, is interpreted as being due to a narrow, random distribution of ligand transfer distances in the heme pocket. This permits evaluation of the most probable recombination rate which is shown to be consistent with ligand tunneling.

MeSH terms

  • Heme*
  • Kinetics
  • Mathematics
  • Models, Chemical
  • Myoglobin*
  • Protein Conformation
  • Structure-Activity Relationship
  • Temperature

Substances

  • Myoglobin
  • Heme