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Related Concept Videos

Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
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Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...

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Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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Quantifying the global cellular thiol-disulfide status.

Rosa E Hansen1, Doris Roth, Jakob R Winther

  • 1Department of Biology, University of Copenhagen, Universitetsparken 13, DK-2100 Copenhagen Ø, Denmark.

Proceedings of the National Academy of Sciences of the United States of America
|January 6, 2009
PubMed
Summary
This summary is machine-generated.

This study reveals that protein thiols, not glutathione, form the primary cellular redox pool. Protein thiols are crucial for cellular defense against oxidative stress.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Oxidative Stress Research

Background:

  • The redox status of protein thiols is critical for protein structure and folding.
  • Glutathione is recognized as a key low-molecular-mass redox regulator.
  • The complete cellular thiol-disulfide balance and relative abundance remain undetermined.

Purpose of the Study:

  • To comprehensively determine the cellular thiol-disulfide status in cultured mammalian cells.
  • To quantify absolute levels of protein thiols, disulfides, and glutathionylated proteins (PSSG).
  • To compare the redox capacity of protein thiols versus glutathione.

Main Methods:

  • Quantification of total cellular thiols and disulfides in all proteins, including membrane proteins.
  • Measurement of reduced and oxidized glutathione levels in the same cells.
  • Assessment of PSSG levels under basal conditions and after exposure to diamide.

Main Results:

  • In HEK and HeLa cells, 6% and 9.6% of total protein cysteines are involved in disulfide bonds, respectively.
  • Steady-state PSSG levels are less than 0.1% of total protein cysteines.
  • Exposure to diamide increased PSSG levels to over 15% of all protein cysteines.

Conclusions:

  • Protein thiols constitute a larger active redox pool than glutathione in mammalian cells.
  • Protein thiols are likely directly involved in cellular defense mechanisms against oxidative stress.
  • This study redefines the roles of protein thiols and glutathione in cellular redox homeostasis.