Product analog binding identifies the copper active site of particulate methane monooxygenase.

ABSTRACT: Nature's primary methane-oxidizing enzyme, the membrane-bound particulate methane monooxygenase (pMMO), catalyzes the oxidation of methane to methanol. pMMO activity requires copper, and decades of structural and spectroscopic studies have sought to identify the active site among three candidates: the Cu_B, Cu_C, and Cu_D sites. Challenges associated with the isolation of active pMMO have hindered progress toward locating its catalytic center. However, reconstituting pMMO into native lipid nanodiscs stabilizes its structure and recovers its activity. Here, these active samples were incubated with 2,2,2,-trifluoroethanol (TFE), a product analog that serves as a readily visualized active-site probe. Interactions of TFE with the Cu_D site were observed

SUBMITTER: Tucci FJ 

PROVIDER: S-EPMC10766429 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature