the variant suppress the conformational change, supporting the involvement in the structural rearrangement. The initial reduction E1/2 in D101Q TauD decreases by 50 mV relative to the wild-type enzyme, reaching comparable values at the end of the reduction. While the initial exponential phase of the oxidationof D101Q is very similar to that of the wild-type protein, oxidation does not continue beyond 100 s
the variant suppress the conformational change, supporting the involvement in the structural rearrangement. Both the reduction and oxidation E1/2 are lower in H255Q TauD than in wild-type enzyme, with no noticeable oxidative reorganization. The reductive reorganization for this protein reaches saturation after 1200 s
the variant shows a larg net redox change relative to the wild-type protein, suggesting that redox-coupled protonation of H99 is required for high redox potentials of the metal
the variant suppress the conformational change, supporting the involvement in the structural rearrangement. The initial reduction E1/2 in D101Q TauD decreases by 50 mV relative to the wild-type enzyme, reaching comparable values at the end of the reduction. While the initial exponential phase of the oxidationof D101Q is very similar to that of the wild-type protein, oxidation does not continue beyond 100 s
the variant suppress the conformational change, supporting the involvement in the structural rearrangement. Both the reduction and oxidation E1/2 are lower in H255Q TauD than in wild-type enzyme, with no noticeable oxidative reorganization. The reductive reorganization for this protein reaches saturation after 1200 s
replacement of the residue that contributes the imidazole ligand cis to the oxo group. Density functional theory calculations show that the imidazole is replaced by a water ligand
the variant shows a larg net redox change relative to the wild-type protein, suggesting that redox-coupled protonation of H99 is required for high redox potentials of the metal