<p>The oxidation of sulfur-containing amino acids, particularly methionine and cysteine, is central to numerous biological processes and is associated with oxidative stress, neurodegenerative diseases such as Parkinson’s and Alzheimer’s, and aging. Methionine sulfoxide reductase (Msr) plays a key role in mitigating oxidative damage by reversing methionine oxidation. This review examines the oxidation of sulfur-containing amino acids and peptides by iron complexes, focusing on their mechanistic pathways via electron transfer or oxygen atom transfer. Kinetic and mechanistic studies highlight the reactivity of methionine, cysteine, and methionine peptides with these oxidants. Density functional theory (DFT) calculations provide insights into the geometry and electronic transitions of metal-salen and oxometal-salen complexes. Electrochemical studies, using differential pulse and cyclic voltammetry, reveal the electrocatalytic properties of L-cysteine, L-methionine, and methionine peptides, demonstrating high sensitivity, low detection limits, and stability. Additionally, the antibacterial activity of Fe(III)-salen complexes is evaluated, identifying minimum inhibitory concentrations against bacterial pathogens. This comprehensive review elucidates the intricate oxidation mechanisms of sulfur amino acids and their relevance in redox chemistry, with implications for biomedical applications.</p>

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State-of-the-Art Oxidation Mechanisms of Sulfur-Containing Amino Acids: Insights into Redox Chemistry, Metal-Ion Catalysis, and Biomedical Implications

  • Karuppiah Nagaraj,
  • Kaliyaperumal Raja,
  • Ramachandran Gokulan,
  • Ukthi Nakshatra,
  • Jayasenthilnathan Abhirami,
  • Swetha Selvaraj,
  • Stenil Sam,
  • Meenakshisundaram Balasubramaniam Lithesh,
  • Mohan Preetham,
  • Chandrasekaran Varshini,
  • Sivaranjani Paramasivam,
  • Shankara Narayanan,
  • Balaji Harish

摘要

The oxidation of sulfur-containing amino acids, particularly methionine and cysteine, is central to numerous biological processes and is associated with oxidative stress, neurodegenerative diseases such as Parkinson’s and Alzheimer’s, and aging. Methionine sulfoxide reductase (Msr) plays a key role in mitigating oxidative damage by reversing methionine oxidation. This review examines the oxidation of sulfur-containing amino acids and peptides by iron complexes, focusing on their mechanistic pathways via electron transfer or oxygen atom transfer. Kinetic and mechanistic studies highlight the reactivity of methionine, cysteine, and methionine peptides with these oxidants. Density functional theory (DFT) calculations provide insights into the geometry and electronic transitions of metal-salen and oxometal-salen complexes. Electrochemical studies, using differential pulse and cyclic voltammetry, reveal the electrocatalytic properties of L-cysteine, L-methionine, and methionine peptides, demonstrating high sensitivity, low detection limits, and stability. Additionally, the antibacterial activity of Fe(III)-salen complexes is evaluated, identifying minimum inhibitory concentrations against bacterial pathogens. This comprehensive review elucidates the intricate oxidation mechanisms of sulfur amino acids and their relevance in redox chemistry, with implications for biomedical applications.