Mirjana B. Colovic, Vesna M. Vasic, Dragan M. Djuric and Danijela Z. Krstic* Pages 324 - 335 ( 12 )
Background: Sulphur is an abundant element in biological systems, which plays an important role in processes essential for life as a constituent of proteins, vitamins and other crucial biomolecules. The major source of sulphur for humans is plants being able to use inorganic sulphur in the purpose of sulphur-containing amino acids synthesis. Sulphur-containing amino acids include methionine, cysteine, homocysteine, and taurine. Methionine and cysteine are classified as proteinogenic, canonic amino acids incorporated in protein structure. Sulphur amino acids are involved in the synthesis of intracellular antioxidants such as glutathione and N-acetyl cysteine. Moreover, naturally occurring sulphur-containing ligands are effective and safe detoxifying agents, often used in order to prevent toxic metal ions effects and their accumulation in human body.
Methods: Literature search for peer-reviewed articles was performed using PubMed and Scopus databases, and utilizing appropriate keywords.
Results: This review is focused on sulphur-containing amino acids – methionine, cysteine, taurine, and their derivatives – glutathione and N-acetylcysteine, and their defense effects as antioxidant agents against free radicals. Additionally, the protective effects of sulphur-containing ligands against the toxic effects of heavy and transition metal ions, and their reactivation role towards the enzyme inhibition are described.
Conclusion: Sulphur-containing amino acids represent a powerful part of cell antioxidant system. Thus, they are essential in the maintenance of normal cellular functions and health. In addition to their worthy antioxidant action, sulphur-containing amino acids may offer a chelating site for heavy metals. Accordingly, they may be supplemented during chelating therapy, providing beneficial effects in eliminating toxic metals.
Antioxidant effects, cysteine, glutathione, heavy metals, methionine, N-acetyl cysteine, taurine.
Department of Physical Chemistry, Institute of Nuclear Sciences “Vinca“, University of Belgrade, Belgrade, Department of Physical Chemistry, Institute of Nuclear Sciences “Vinca“, University of Belgrade, Belgrade, Institute of Medical Physiology “Richard Burian”, Faculty of Medicine, University of Belgrade, Belgrade, Institute of Medical Chemistry, Faculty of Medicine, University of Belgrade, Belgrade