Sulfenic acid in human serum albumin.

  • Turell L
  • Botti H
  • Carballal S
 et al. 
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Abstract

Sulfenic acid (RSOH) is a central intermediate in both the reversible and irreversible redox modulation by reactive species of an increasing number of proteins involved in signal transduction and enzymatic pathways. In this paper we focus on human serum albumin (HSA), the most abundant plasma protein, proposed to serve antioxidant functions in the vascular compartment. Sulfenic acid in HSA has been previously detected using different methods after oxidation of its single free thiol Cys34 through one- or two-electron mechanisms. Since recent evidence suggests that sulfenic acid in HSA is stabilized within the protein environment, this derivative represents an appropriate model to examine protein sulfenic acid biochemistry, structure and reactivity. Sulfenic acid in HSA could be involved in mixed disufide formation, supporting a role of HSA-Cys34 as an important redox regulator in extracellular compartments.

Author-supplied keywords

  • free radicals
  • free radicals metabolism
  • humans
  • models
  • molecular
  • oxidants
  • oxidation reduction
  • protein conformation
  • serum albumin
  • serum albumin chemistry
  • serum albumin metabolism
  • sulfenic acids
  • sulfenic acids isolation & purification
  • sulfenic acids metabolism

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  • PMID: 17061035

Authors

  • Lucía Turell

  • Horacio Botti

  • Sebastián Carballal

  • Gerardo Ferrer-Sueta

  • José M Souza

  • Rosario Durán

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