Structural and electronic modulations of lytic polysaccharide monooxygenase (LPMO) upon chitin binding: insights from X-ray spectroscopy.

ABSTRACT: Lytic polysaccharide monooxygenases (LPMOs) play a critical role in the depolymerization of recalcitrant polysaccharides, such as chitin, making them of interest in biotechnological applications. These interfacial enzymes are also of great chemical interest because of their unique monocopper catalytic center and their ability to activate high energy C-H bonds. This report investigates the structural and electronic changes at the copper (Cu) site of an LPMO, SmAA10A, upon binding of its chitin substrate, utilizing a suite of spectroscopic and computational methods. Herein, we present the first reported X-ray Absorption (XAS) and Emission (XES) spectroscopic data on substrate-bound LPMO. By comparing the Cu(ii) and Cu(i) states of SmAA10A in both the chitin-bound and unbound st

SUBMITTER: Joseph C 

PROVIDER: S-EPMC12658904 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature