BECAS
PALERMO Juan Cruz
congresos y reuniones científicas
Título:
Disulfane-mediated reduction of metmyoglobin
Autor/es:
PALERMO, JUAN CRUZ; CARLLINNI COLOMBO, MELISA; SCOCOZZA, MAGALÍ; MURGIDA, DANIEL H.; BOUBETA, FERNANDO MARTÍN; ESTRIN, DARÍO ARIEL; BARI, SARA ELIZABETH
Lugar:
Roma
Reunión:
Congreso; International hybrid Conference on Oxygen Binding and Sensing Proteins; 2022
Institución organizadora:
Universidad de Roma
Resumen:
Dihydrogen disulfane, H2S2, is an endogenous species that has been reported as effector of the biochemical activity of hydrogen sulfide, H2S, in certain tissues.The metal centered reduction of the heme protein indoleamine 2,3 dioxygenase by disodium disulfane, Na2S2, leading to a potent activation of the enzyme, precedes and highlights the interest of heme proteins as biochemical targets of disulfane species.2 Herein, we focused on the reactivity of H2S2, or the conjugated base HSS¯, towards metmyoglobin, MbFeIII .The reaction of excess Na2S2 with MbFeIII, was studied under argon atmosphere at 25ºC. A fast biexponential formation of MbFeII was observed by UV-Vis spectroscopy in the interval 6