Cu site differentiation in tetracopper(i) sulfide clusters enables biomimetic N₂O reduction.

ABSTRACT: Copper clusters feature prominently in both metalloenzymes and synthetic nanoclusters that mediate catalytic redox transformations of gaseous small molecules. Such reactions are critical to biological energy conversion and are expected to be crucial parts of renewable energy economies. However, the precise roles of individual metal atoms within clusters are difficult to elucidate, particularly for cluster systems that are dynamic under operating conditions. Here, we present a metal site-specific analysis of synthetic Cu₄(μ₄-S) clusters that mimic the Cu _Z active site of the nitrous oxide reductase enzyme. Leveraging the ability to obtain structural snapshots of both inactive and active forms of the synthetic model system, we analyzed both states usin

SUBMITTER: Alayoglu P 

PROVIDER: S-EPMC11306996 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature