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Nitric Oxide Destroys Zinc-Sulfur Clusters Inducing Zinc Release from Metallothionein and Inhibition of the Zinc Finger-Type Yeast Transcription Activator LAC9

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Abstract

Nitric oxide, generated from S-nitrosocysteine or applied as gas mediates metal ion release from the Zn2+/Cd2+-complexing protein metallothionein via oxidation of SH-groups. Time-dependent S-nitrosylation and subsequent disulfide formation of metallothionein are demonstrated. Furthermore, nitric oxide inhibits DNA binding activity of the yeast transcription factor LAC9 containing a zinc finger like DNA binding domain. These results show that nitric oxide interacts with and destroys zinc-sulfur clusters in proteins.

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