A De Novo Designed Trimeric Metalloprotein as a Ni_p Model of the Acetyl-CoA Synthase.

ABSTRACT: We present a Ni_p site model of acetyl coenzyme-A synthase (ACS) within a de novo-designed trimer peptide that self-assembles to produce a homoleptic Ni(Cys)₃ binding motif. Spectroscopic and kinetic studies of ligand binding demonstrate that Ni binding stabilizes the peptide assembly and produces a terminal Ni^I-CO complex. When the CO-bound state is reacted with a methyl donor, a new species is quickly produced with new spectral features. While the metal-bound CO is albeit unactivated, the presence of the methyl donor produces an activated metal-CO complex. Selective outer sphere steric modifications demonstrate that the physical properties of the ligand-bound states are altered differently depending on the location of the steric modification above or below the Ni site.

SUBMITTER: Selvan D 

PROVIDER: S-EPMC10299331 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature