Heme iron as target of Hydrodisulfide

JUAN CRUZ PALERMO; DARIO A. ESTRIN; FERNANDO MARTÍN BOUBETA; MELISA CARLLINNI COLOMBO; SARA E. BARI

Montevideo

Simposio; Redox Chemistry and Biology of Thiols. Course and Symposium; 2019

Instituto Pasteur

Hydrogen polysulfides, H2Sn (n>1), are gaining growing interest because some of the physiological roles formerly attributed to endogenous hydrogen sulfide, H2S, are better described as a consequence of their more potent action.H2Sn (n=2,3) have been demonstrated to be products of the H2S forming enzyme, the 3-mercaptopyruvate sulfurtransferase. The interaction of related low molecular weight persulfide species (RSSnH, n=1) with ferric hemeproteins as potential targets of biochemical interest has been recently explored, and the metal center reduction or the coordination have been reported as products.We present herein a study of the kinetics of the interaction of disodium disulfane, Na2S2, with metmyoglobin (FeIIIMb) at neutral pH, and a comparison with the results previously reported using Na2S.