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

Academic Article
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Overview

authors

  • Jeng, M. F.
  • Reymond, M. T.
  • Tennant, L. L.
  • Holmgren, A.
  • Dyson, Jane

publication date

  • October 1998

journal

  • European Journal of Biochemistry  Journal

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we have prepared a mutant of Escherichia coli thioredoxin where the second cysteine residue of the active site has been replaced by an alanine residue.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 residue and a short cysteine-containing peptide. This paper describes the preparation and characterization of the mutant protein both free and in the peptide complex.

subject areas

  • Amino Acid Sequence
  • Cysteine
  • Escherichia coli
  • Hydrogen-Ion Concentration
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Protein Conformation
  • Thioredoxins
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Research

keywords

  • mixed disulfide
  • reduction mechanism
  • thioredoxin
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Identity

International Standard Serial Number (ISSN)

  • 0014-2956

Digital Object Identifier (DOI)

  • 10.1046/j.1432-1327.1998.2570299.x

PubMed ID

  • 9826174
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Additional Document Info

start page

  • 299

end page

  • 308

volume

  • 257

issue

  • 2

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