Key result
S-nitrosation of the zinc tetrathiolate cysteine by NO donors resulted in zinc release from the dimer interface and formation of inactive iNOS monomers.
Population
Escherichia coli expressing wild-type inducible nitric oxide synthase and zinc tetrathiolate mutants, and…
Comparison
NO donor (DEA/NO) vs Control sample
Design
Preclinical
Authors
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Zinc-free single mutants retain activity; leaves open zinc's role in iNOS and requires mammalian validation.
S-nitrosation of the zinc tetrathiolate cysteine in iNOS causes zinc release and enzyme inactivation via monomer formation, revealing a potential physiological regulatory mechanism.
Mitchell et al. (2005) studied this question. DEA/NO (NO donor) vs. Control sample was evaluated on Zinc content and iNOS activity. S-nitrosation of the zinc tetrathiolate cysteine by NO donors resulted in zinc release from the dimer interface and formation of inactive iNOS monomers.
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