Structural Dynamics of the Methyl-Coenzyme M Reductase Active Site Are Influenced by Coenzyme F₄₃₀ Modifications.

ABSTRACT: Methyl-coenzyme M reductase (MCR) is a central player in methane biogeochemistry, governing methanogenesis and the anaerobic oxidation of methane (AOM) in methanogens and anaerobic methanotrophs (ANME), respectively. The prosthetic group of MCR is coenzyme F₄₃₀, a nickel-containing tetrahydrocorphin. Several modified versions of F₄₃₀ have been discovered, including the 17²-methylthio-F₄₃₀ (mtF₄₃₀) used by ANME-1 MCR. Here, we employ molecular dynamics (MD) simulations to investigate the active site dynamics of MCR from Methanosarcina acetivorans and ANME-1 when bound to the canonical F₄₃₀ compared to 17²-thioether coenzyme F₄₃₀ variants and substrates (methyl-coenzyme M and coenzyme B) for methan

SUBMITTER: Poleto MD 

PROVIDER: S-EPMC11256747 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature