NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex

Mei Fen Jeng, Martine T. Reymond, Linda L. Tennant, Arne Holmgren, H. Jane Dyson

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

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we have prepared a mutant of Escherichia coli thioredoxin where the second cysteine residue of the active site has been replaced by an alanine residue.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.

Original languageEnglish
Pages (from-to)299-308
Number of pages10
JournalEuropean Journal of Biochemistry
Volume257
Issue number2
DOIs
Publication statusPublished - 1998 Oct 15

All Science Journal Classification (ASJC) codes

  • Biochemistry

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