Nitric Oxide Interacting with Glutathione Transferases

Abstract

This short review deals with nitric oxide interacting with proteins (e.g., glutathione transferases) in the presence of GSH and iron. GST P1-1 may act as a NO carrier protein when GSH depletion occurs in the cell. Conversely, in the presence of GSH and traces of ferrous ions, the new formed dinitrosyl-diglutathionyl-iron complexes (DNDGICs) may act as activity modulators with GST P1-1 through competitive inhibition and as strong oxidants with glutathione reductase through irreversible inhibition. DNICs formation inside the cell is followed by a strong interaction with a number of proteins including GSTs and has been object of a number of papers where the most recently evolved GSTs bind DNICs..