Article
H93G myoglobin cavity mutant as versatile template for modeling heme proteins: magnetic circular dichroism studies of thiolate- and imidazole-ligated complexes.
Biopolymers - 1 Jan 2002
Dawson John H, Pond Alycen E, Roach Mark P
Abstract excerpt
Recent ligand binding and spectroscopic investigations of the myoglobin H93G cavity mutant are reviewed, revealing it to be a versatile template for the preparation of model heme complexes of defined structure. The H93G myoglobin cavity mutant is shown to be capable of forming mixed ligand adducts because of the difference in accessibility of the two sides of the ferric heme iron. With imidazole bound in the...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.