This study addresses potential molecular mechanisms underlying the inhibition of the
transcription factor c-Jun by nitric oxide. We show that in the presence of the physiological
sulfhydryl glutathione nitric oxide modifies the two cysteine residues contained in the DNA
binding module of c-Jun in a selective and distinct way. Although nitric oxide induced the
formation of an intermolecular disulfide bridge between cysteine residues in the leucine
zipper site of c-Jun monomers, this same radical directed the covalent incorporation of …