Journal
FREE RADICAL BIOLOGY AND MEDICINE
Volume 80, Issue -, Pages 148-157Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.freeradbiomed.2014.11.013
Keywords
Cysteine; Redox regulation; Thiols; pK(a); Redox potential; Free radicals
Funding
- National Institutes of Health [R01 GM050389, R33 CA177461]
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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 to functional sites 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 pK(a) 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. (C) 2014 Elsevier Inc. All rights reserved.
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