Steady-state kinetic studies of glutathione reductase

Abstract

The steady-state kinetic studies of yeast glutathione reductase, performed when [GSSG] = 10[NADPH] in the assay mixture, show that at concentrations of GSSG under 450 microM the enzymatic mechanism pathway is ping-pong.Furthermore, in the case of higher values, the enzymatic kinetics follows a sequential pathway.However when the glutathione reductase reaction passes to the ping-pong mechanism, the inhibition effect by excess of NADPH is stronger than when the reaction takes place over the sequential mechanism.