Cu₄S Cluster in "0-Hole" and "1-Hole" States: Geometric and Electronic Structure Variations for the Active Cu_Z* Site of N₂O Reductase.

ABSTRACT: The active site of nitrous oxide reductase (N₂OR), a key enzyme in denitrification, features a unique μ₄-sulfido-bridged tetranuclear Cu cluster (the so-called Cu_Z or Cu_Z* site). Details of the catalytic mechanism have remained under debate and, to date, synthetic model complexes of the Cu_Z*/Cu_Z sites are extremely rare due to the difficulty in building the unique {Cu₄(μ₄-S)} core structure. Herein, we report the synthesis and characterization of [Cu₄(μ₄-S)]ⁿ⁺ (n = 2, 2; n = 3, 3) clusters, supported by a macrocyclic {py₂NHC₄} ligand (py = pyridine, NHC = N-heterocyclic carbene), in both their 0-hole (2) and

SUBMITTER: Liu Y 

PROVIDER: S-EPMC10450684 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature