AI Article Synopsis
- In mitochondria, excess hydrogen sulfide (HS) is detoxified through an oxidation process facilitated by the enzyme SOD1, which uses copper and zinc.
- The study introduces synthetic Ni(II) complexes with a terminal SH group as alternatives to SOD1 for sulfide oxidation.
- The synthesis, structure, and spectroscopic analysis of these complexes were detailed, and their catalytic reactions were evaluated under anaerobic conditions, comparing their reactivity to that of the native SOD1 enzyme.
Article Abstract
In mitochondria, the detoxification of molar excess HS as polysulfide proceeded an oxidation process promoted by Cu/Zn containing superoxide dismutase (SOD1) enzyme, which has been very recently reported as the alternative enzyme for cytosolic HS oxidation. Herein, we present Ni(II) complexes bearing the terminal SH group as a synthetic functional analogue for the sulfide oxidase function of SOD1. Synthesis, crystal structure and complete spectroscopic characterization of two sets of complexes, [NiL(PPh)] (2OMe/tBu) and tetraethyl salt of [NiL(SH)] (3OMe/tBu), were described (LOMe = ()-2-methoxy-6-(((2-sulfidophenyl)imino)methyl)phenolate and LtBu = ()-2,4-di--butyl-6-(((2-sulfidophenyl)imino)methyl)phenolate). Under anaerobic conditions, 3OMe/tBu responded to a catalytic sulfur atom transfer (SAT) reaction with PPh to produce SPPh. The SAT reaction was analyzed using detailed studies of H and P NMR spectra. Finally, the SAT reactivity pattern was compared with the same in the native enzyme of SOD1.
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| http://dx.doi.org/10.1039/d4dt01364f | DOI Listing |
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