The Basics of Thiols and Cysteines in Redox Biology and Chemistry
By Leslie B. Poole. Free Radical Biology & Medicine, 2014
876 citations recorded by the source corpus.
Cysteine is one of the least abundant amino acids, yet it is frequently found as a highly conserved residue within functional (regulatory, catalytic or binding) sites in proteins. It is the unique chemistry of the thiol or thiolate group of cysteine that imparts functional sites with their specialized properties (e.g., nucleophilicity, high affinity metal binding, and/or ability to form disulfide bonds). Highlighted in this review are some of the basic biophysical and biochemical properties of cysteine groups and the equations that apply to them, particularly with respect to pKa and redox potential. Also summarized are the types of low molecular weight thiols present in high concentrations in most cells, as well as the ways in which modifications of cysteinyl residues can impart or regulate molecular functions important to cellular processes including signal transduction.
Subfields: Biochemistry, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/5216bbd1bd95947576a905555c1f525dc7b38b2b
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Biochemistry
In Molecular Biology
Citations in the corpus
- Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans (2017, background): “The primary product of cysteine residue oxidation by H2O2 is the sulfenic acid (−SOH), whose stability and further reactivity may be influenced by the presence or availability of a proximal thiol group, resulting in the formationof a disulfide bond[281, 282] (Figure 3).”