The mechanism of disulfide reduction by thioredoxin in the cell is thought to occur through the formation and subsequent destruction of a mixed- disulfide intermediate between thioredoxin and the substrate. In order to model the interaction, we have prepared a mutant of Escherichia coli thioredoxin where the second cysteine residue of the active site has been replaced by an alanine residue. A specific covalent complex has been prepared between the remaining cysteine-containing peptide. This paper describes the preparation and characterization off the mutant protein both free and in the peptide complex.
|Number of pages||10|
|Journal||European Journal of Biochemistry|
|Publication status||Published - 1998 Oct 15|
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