Low-molecular-weight thiols in thiol-disulfide exchange.

TitleLow-molecular-weight thiols in thiol-disulfide exchange.
Publication TypeJournal Article
Year of Publication2013
AuthorsVan Laer, K., C. J. Hamilton, and J. Messens
JournalAntioxid Redox Signal
Volume18
Issue13
Pagination1642-53
Date Published2013 May 01
Type of Articleredox
ISSN1557-7716
KeywordsDisulfides, Kinetics, Molecular Weight, Oxidation-Reduction, Oxidative Stress, Sulfhydryl Compounds
Abstract

SIGNIFICANCE: Oxidative stress is widely invoked in inflammation, aging, and complex diseases. To avoid unwanted oxidations, the redox environment of cellular compartments needs to be tightly controlled. The complementary action of oxidoreductases and of high concentrations of low-molecular-weight (LMW) nonprotein thiols plays an essential role in maintaining the redox potential of the cell in balance.RECENT ADVANCES: While LMW thiols are central players in an extensive range of redox regulation/metabolism processes, not all organisms use the same thiol cofactors to this effect, as evidenced by the recent discovery of mycothiol (MSH) and bacillithiol (BSH) among different gram-positive bacteria.CRITICAL ISSUES: LMW thiol-disulfide exchange processes and their cellular implications are often oversimplified, as only the biology of the free thiols and their symmetrical disulfides is considered. In bacteria under oxidative stress, especially where concentrations of different LMW thiols are comparable [e.g., BSH, coenzyme A (CoA), and cysteine (Cys) in many low-G+C gram-positive bacteria (Firmicutes)], mixed disulfides (e.g., CoASSB and CySSCoA) must surely be major thiol-redox metabolites that need to be taken into consideration.FUTURE DIRECTIONS: There are many microorganisms whose LMW thiol-redox buffers have not yet been identified (either bioinformatically or experimentally). Many elements of BSH and MSH redox biochemistry remain to be explored. The fundamental biophysical properties, thiol pK(a) and redox potential, have not yet been determined, and the protein interactome in which the biothiols MSH and BSH are involved needs further exploration.

DOI10.1089/ars.2012.4964
Alternate JournalAntioxid. Redox Signal.
PubMed ID23075082
Grant ListBB/H013504/1 / / Biotechnology and Biological Sciences Research Council / United Kingdom
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