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we have prepared a mutant of Escherichia coli thioredoxin where the second cysteine residue of the active site has been replaced by an alanine residue.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.
|頁（從 - 到）||299-308|
|期刊||European Journal of Biochemistry|
|出版狀態||Published - 1998 十月 15|
All Science Journal Classification (ASJC) codes