Ligand migration pathway and protein dynamics in myoglobin: a time-resolved crystallographic study on L29W MbCO.

ABSTRACT: By using time-resolved x-ray crystallography at room temperature, structural relaxations and ligand migration were examined in myoglobin (Mb) mutant L29W from nanoseconds to seconds after photodissociation of carbon monoxide (CO) from the heme iron by nanosecond laser pulses. The data were analyzed in terms of transient kinetics by fitting trial functions to integrated difference electron density values obtained from select structural moieties, thus allowing a quantitative description of the processes involved. The observed relaxations are linked to other investigations on protein dynamics. At the earliest times, the heme has already completely relaxed into its domed deoxy structure, and there is no photo-dissociated CO visible at the primary docking site. Initial relaxations of larger glo

SUBMITTER: Schmidt M 

PROVIDER: S-EPMC1187994 | biostudies-literature | 2005 Aug

REPOSITORIES: biostudies-literature