X-ray-induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner.

ABSTRACT: Since the advent of protein crystallography, atomic-level macromolecular structures have provided a basis to understand biological function. Enzymologists use detailed structural insights on ligand coordination, interatomic distances, and positioning of catalytic amino acids to rationalize the underlying electronic reaction mechanisms. Often the proteins in question catalyze redox reactions using metal cofactors that are explicitly intertwined with their function. In these cases, the exact nature of the coordination sphere and the oxidation state of the metal is of utmost importance. Unfortunately, the redox-active nature of metal cofactors makes them especially susceptible to photoreduction, meaning that information obtained by photoreducing X-ray sources about the environment of the cofa

SUBMITTER: Pfanzagl V 

PROVIDER: S-EPMC7521648 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature