Selective oxidation of active site aromatic residues in engineered Cu proteins.

ABSTRACT: Recent studies have revealed critical roles for the local environments surrounding metallocofactors, such as the newly identified Cu_D site in particulate methane monooxygenases (pMMOs) and the second sphere aromatic residues in lytic polysaccharide monooxygenases (LPMOs), implicated in the protection against oxidative damage. However, these features are subjects of continued debate. Our work utilizes biotin-streptavidin (Sav) technology to develop artificial metalloproteins (ArMs) that mimic the active sites of natural copper metalloenzymes. By engineering ArMs with aromatic residues within their secondary coordination spheres, we systematically investigate the influence of these residues on Cu reactivity and oxidant activation. We demonstrate that the placement and orientation

SUBMITTER: Uyeda KS 

PROVIDER: S-EPMC11587884 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature