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Lactic acid and glutathione (still bound to metal 2 as a thiolate) are formed

In conclusion, we established and applied a roGFP2-based assay to rapidly screen for gain- or loss-of-function mutants of Grx isoforms in yeast, quantified the relevance and contribution of four crucial protein areas for the oxidative and reductive half-reaction of Grx catalyis, show that the flanking lysine and tyrosine residue do not affect the thiol p K a value of the active-site cysteine residue but rather stabilize the transition states, and propose an active-site loop-dependent conformational on/off switch that inactivates class II Grx in the absence of ironsulfur clusters

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