Mechanistic insight into hydroxamate transfer reaction mimicking the inhibition of zinc-containing enzymes

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A hydroxamate transfer reaction between metal complexes has been investigated by a combination of experimental and theoretical studies. A hydroxamate-bound cobalt(ii) complex bearing a tetradentate macrocyclic ligand, [Co-II(TBDAP)(CH3C(-NHO)O)](+)(1), is prepared by the reduction of a hydroximatocobalt(iii) complex with a biological reductant. Alternatively,1is accessibleviaa synthetic route for the reaction between the cobalt(ii) complex and acetohydroxamic acid in the presence of a base.1was isolated and characterized by various physicochemical methods, including UV-vis, IR, ESI-MS, and X-ray crystallography. The hydroxamate transfer reactivity of1was examined with a zinc complex, which was followed by UV-vis and ESI-MS. Kinetic and activation parameter data suggest that the hydroxamate transfer reaction occursviaa bimolecular mechanism, which is also supported by DFT calculations. Moreover,1is able to inhibit the activity against a zinc enzyme,i.e., matrix metalloproteinase-9. Our overall investigations of the hydroxamate transfer using the synthetic model system provide considerable insight into the final step involved in the inhibition of zinc-containing enzymes.
Publisher
ROYAL SOC CHEMISTRY
Issue Date
2020-09
Language
English
Article Type
Article
Citation

CHEMICAL SCIENCE, v.11, no.33, pp.9017 - 9021

ISSN
2041-6520
DOI
10.1039/d0sc02676j
URI
http://hdl.handle.net/10203/276375
Appears in Collection
CH-Journal Papers(저널논문)
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