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In the absence of its substrate, the autoreduction of the high-valent bis-Fe IV state of the hemes of MauG to the diferric state proceeds via a Compound I-like and then a Compound II-like intermediate. This process is coupled to oxidative damage to specific methionine residues and inactivation of MauG. The autoreduction of a P107V MauG variant, which is more prone to oxidative damage, proceeds directly from the bis-Fe IV to the Compound II-like state with no detectable Compound I intermediate. Comparison of the crystal structures of native and P107V MauG reveals that this mutation alters the positions of amino acid residues in the heme site as well as the water network that delivers protons from the solvent to the hemes during their reduction. Kinetic, spectroscopic, and solvent kinetic isotope effect studies demonstrate that these changes in the heme site affect the protonation state of the ferryl heme and the relative efficiencies of two alternative pathways for the transfer of protons from solvent to the hemes. These changes enhance the rate of autoreduction of P107V MauG such that it competes with the catalytic reaction with substrate and causes the enzyme to inactivate itself during the steady-state reaction with H 2 O 2 and its substrate. Thus, while this mutation has negligible effects on the initial steady-state kinetic parameters of MauG, it is a fatal mutation as it causes inactivation during catalysis.

A Suicide Mutation Affecting Proton Transfers to High-Valent Hemes Causes Inactivation of MauG during Catalysis