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Related Concept Videos

Preparation and Reactions of Sulfides02:26

Preparation and Reactions of Sulfides

5.9K
Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.
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Structure and Nomenclature of Thiols and Sulfides02:17

Structure and Nomenclature of Thiols and Sulfides

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Thiols and sulfides are sulfur analogs of alcohols and ethers, respectively, where the sulfur atom takes the place of the oxygen atom. Thus, thiols are generally represented as RSH, where R is an alkyl substituent and —SH is the functional group. On the other hand, in sulfides, the central sulfur atom is bonded to two hydrocarbon groups on either side. Depending upon the type of group, sulfides can be either symmetrical or asymmetrical. Both thiols and sulfides display a bent geometry,...
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Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

7.9K
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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Exceptions to the Octet Rule02:55

Exceptions to the Octet Rule

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Many covalent molecules have central atoms that do not have eight electrons in their Lewis structures. These molecules fall into three categories:
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Sulfur Assimilation01:20

Sulfur Assimilation

482
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...
482
Microbes and the Sulfur Cycle01:29

Microbes and the Sulfur Cycle

20
Sulfur is a vital element in Earth's biogeochemical systems. It transitions through various inorganic states, including sulfate (SO₄²⁻), elemental sulfur (S⁰), and sulfide (S²⁻). Abiotic and biological mechanisms across oxic and anoxic environments intricately mediate these transformations. Sulfate, the most oxidized form of sulfur, is predominantly stored in rocks, marine sediments, and oceanic waters, acting as a long-term reservoir in the global sulfur...
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Updated: Mar 22, 2026

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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Mixed results with mixed disulfides.

Regina Brigelius-Flohé1

  • 1German Institute of Human Nutrition Potsdam-Rehbruecke, Arthur-Scheunert-Allee 114-116, 14558 Nuthetal, Germany.

Archives of Biochemistry and Biophysics
|April 21, 2016
PubMed
Summary

Research in the 1980s explored metabolic changes from oxidative stress in perfused organs. Key findings revealed alterations in the glutathione system and protein glutathionylation, a vital redox biology mechanism.

Keywords:
Glucose-6-phosphate dehydrogenaseGlutathionylationMixed disulfidesNitrofurantoinParaquatProtein thiols

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Area of Science:

  • Redox Biology
  • Metabolic Biochemistry

Background:

  • Oxidative challenges significantly impact cellular metabolism.
  • The glutathione and NADPH/NADP+ systems are crucial in managing oxidative stress.
  • Understanding metabolic alterations under near-physiological conditions is vital.

Purpose of the Study:

  • To investigate metabolic changes in perfused organs under oxidative stress.
  • To analyze alterations in the glutathione and NADPH/NADP+ systems.
  • To explore the formation and significance of glutathione mixed disulfides with proteins.

Main Methods:

  • Experiments utilized perfused organs to mimic near-physiological conditions.
  • Focused on analyzing the glutathione and NADPH/NADP+ systems.
  • Adapted and employed a specific assay for detecting glutathione mixed disulfides.

Main Results:

  • Observed significant alterations in the glutathione and NADPH/NADP+ systems due to oxidants.
  • Identified the formation of glutathione mixed disulfides with proteins.
  • Preliminary evidence suggested potential activation of glutathione-6-phosphate dehydrogenase (G6PDH) by glutathionylation.

Conclusions:

  • Glutathionylation of proteins is a key posttranslational modification in redox biology.
  • Early studies laid groundwork for understanding redox regulation of enzyme activity.
  • The adapted assay for mixed disulfides remains relevant in current research.