Abstract
Sulfitolysis of wild-type and four mutated Escherichia coli thioredoxins ([D26A]thioredoxin, [P34H]thioredoxin, [K36E]thioredoxin and endo-Arg33a-thioredoxin) has been investigated at millimolar concentrations of sulfite in the absence of protein-denaturing agents by fluorescence spectroscopy. Sulfitolysis of the single disulfide bridge of these proteins is associated with an increase in fluorescence emissions at 345 nm. Evaluation of the fluorescence emission spectra revealed that sulfitolysis of thioredoxins is a homogenous process. The reactivities of the thioredoxins are determined by negatively charged (Asp26) or positively charged (Lys36) amino acid residues near the active site disulfide bridge.
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