Mixed Valence {Ni²⁺Ni¹⁺} Clusters as Models of Acetyl Coenzyme A Synthase Intermediates.

ABSTRACT: Acetyl coenzyme A synthase (ACS) catalyzes the formation and deconstruction of the key biological metabolite, acetyl coenzyme A (acetyl-CoA). The active site of ACS features a {NiNi} cluster bridged to a [Fe₄S₄]ⁿ⁺ cubane known as the A-cluster. The mechanism by which the A-cluster functions is debated, with few model complexes able to replicate the oxidation states, coordination features, or reactivity proposed in the catalytic cycle. In this work, we isolate the first bimetallic models of two hypothesized intermediates on the paramagnetic pathway of the ACS function. The heteroligated {Ni²⁺Ni¹⁺} cluster, [K(12-crown-4)₂][1], effectively replicates the coordination number and oxidation state of the proposed "A<

SUBMITTER: Wilson DWN 

PROVIDER: S-EPMC11295191 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature