Host: The Japanese Society of Toxicology
Cysteine-bound sulfane sulfur in proteins has received much attention as a key factor in cellular redox homeostasis. With an established method to quantify protein-bound sulfane sulfur, metallothionen (MT) isoforms were found to be highly modified by sulfane sulfur with C-S-S-Zn structure which is supported by Raman spectroscopy and a 3D structure modeling analysis. Evaluation of redox-dependent zinc and sulfane sulfur binding in MT3 suggest that oxidation of zinc/sulfur cluster in MT3 yields intramolecular tetrasulfide bridges coupled to zinc release from the protein. In the symposium, we will introduce the function of sulfane sulfur in the redox regulation of MT proteins.
