X-ray snapshots reveal conformational influence on active site ligation during metalloprotein folding.

ABSTRACT: Cytochrome c (cyt c) has long been utilized as a model system to study metalloprotein folding dynamics and the interplay between active site ligation and tertiary structure. However, recent reports regarding the weakness of the native Fe(ii)-S bond (Fe-Met80) call into question the role of the active site ligation in the protein folding process. In order to investigate the interplay between protein conformation and active site structures, we directly tracked the evolution of both during a photolysis-induced folding reaction using X-ray transient absorption spectroscopy and time-resolved X-ray solution scattering techniques. We observe an intermediate Fe-Met80 species appearing on ∼2 μs timescale, which should not be sustained without stabilization from the folded protein stru

SUBMITTER: Hsu DJ 

PROVIDER: S-EPMC6993610 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature