Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of Fe^IV = O formation in bacterial dye-decolorizing peroxidases.

ABSTRACT: Structure determination of proteins and enzymes by X-ray crystallography remains the most widely used approach to complement functional and mechanistic studies. Capturing the structures of intact redox states in metalloenzymes is critical for assigning the chemistry carried out by the metal in the catalytic cycle. Unfortunately, X-rays interact with protein crystals to generate solvated photoelectrons that can reduce redox active metals and hence change the coordination geometry and the coupled protein structure. Approaches to mitigate such site-specific radiation damage continue to be developed, but nevertheless application of such approaches to metalloenzymes in combination with mechanistic studies are often overlooked. In this review, we summarize our recent structural and kinetic studi

SUBMITTER: Lucic M 

PROVIDER: S-EPMC8463360 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature