Methionine oxidation and reduction in proteins

Biochim Biophys Acta. 2014 Feb;1840(2):901-5. doi: 10.1016/j.bbagen.2013.04.038. Epub 2013 May 3.

Abstract

Background: Cysteine and methionine are the two sulfur containing amino acids in proteins. While the roles of protein-bound cysteinyl residues as endogenous antioxidants are well appreciated, those of methionine remain largely unexplored.

Scope: We summarize the key roles of methionine residues in proteins.

Major conclusion: Recent studies establish that cysteine and methionine have remarkably similar functions.

General significance: Both cysteine and methionine serve as important cellular antioxidants, stabilize the structure of proteins, and can act as regulatory switches through reversible oxidation and reduction. This article is part of a Special Issue entitled Current methods to study reactive oxygen species - pros and cons and biophysics of membrane proteins. Guest Editor: Christine Winterbourn.

Keywords: A(2)M; MetO; Methionine; Methionine sulfoxide; Methionine sulfoxide reductase; Msr; Oxidant defense; methionine sulfoxide; methionine sulfoxide reductase; α(2)macroglobulin.

Publication types

  • Review

MeSH terms

  • Animals
  • Humans
  • Methionine / chemistry*
  • Oxidation-Reduction
  • Proteins / chemistry*

Substances

  • Proteins
  • Methionine