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Related Concept Videos

Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

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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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Preparation and Reactions of Sulfides02:26

Preparation and Reactions of Sulfides

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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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Sulfur Assimilation01:20

Sulfur Assimilation

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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...
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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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Electrophilic Aromatic Substitution: Sulfonation of Benzene01:22

Electrophilic Aromatic Substitution: Sulfonation of Benzene

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Sulfonation of benzene is a reaction wherein benzene is treated with fuming sulfuric acid at room temperature to produce benzenesulfonic acid. Fuming sulfuric acid is a mixture of sulfur trioxide and concentrated sulfuric acid.
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Oxidation and Reduction of Organic Molecules01:19

Oxidation and Reduction of Organic Molecules

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Energy production within a cell involves many coordinated chemical pathways. Most of these pathways are combinations of oxidation and reduction reactions, which occur at the same time. An oxidation reaction strips an electron from an atom in a compound, and the addition of this electron to another compound is a reduction reaction. Because oxidation and reduction usually occur together, these pairs of reactions are called redox reactions.
The removal of an electron from a molecule, results in a...
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Force-Triggered Thermodynamically Uphill Disulfide Reduction through Sulfur Oxidation State Control.

Marc Mora1,2, Georgia Cohen1,2, William Cranton1,2

  • 1Department of Physics, Randall Centre for Cell and Molecular Biophysics, Centre for the Physical Science of Life and London Centre for Nanotechnology, King's College London, Strand, London WC2R 2LS, U.K.

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Summary
This summary is machine-generated.

Mechanical forces can activate chemical reactions, including the reduction of protein disulfide bonds by inorganic oxyanions. This force-unlocked reactivity impacts protein elasticity, revealing new mechanochemical pathways.

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Area of Science:

  • Mechanochemistry
  • Biophysics
  • Protein Science

Background:

  • Mechanical forces, alongside thermal energy, current, and light, can activate chemical reactions and alter reaction pathways.
  • Single-molecule mechanochemistry has shown that force accelerates bond scission and ring-opening in polymers.
  • The SN2 thiol-disulfide reaction is a model for studying force-dependent nucleophilic substitution, but the reactivity of inorganic sulfur-oxyanions is less understood.

Purpose of the Study:

  • To investigate whether mechanical forces can activate the rupture of protein disulfide bonds by inorganic sulfur-oxyanions.
  • To explore the force-dependent reactivity of thermodynamically nonfavored reactions involving protein disulfide bonds.

Main Methods:

  • Single-molecule force-clamp spectroscopy to measure force-dependent reaction rates.
  • Density functional theory (DFT) calculations to model reaction mechanisms.
  • Colorimetric assay measurements to quantify reaction outcomes.

Main Results:

  • Demonstrated that mechanical force can activate the thermodynamically nonfavored reduction of disulfide bonds by inorganic oxyanions.
  • Showed that this force-activated reactivity occurs within the protein core, impacting proteins with physiological mechanical roles.
  • Quantified the direct impact of force-unlocked disulfide bond rupture on protein elasticity.

Conclusions:

  • Mechanical force can overcome thermodynamic barriers to activate disulfide bond reduction by less reactive inorganic oxyanions.
  • This mechanochemical activation has significant implications for understanding protein mechanics and function under force.
  • The findings reveal a novel pathway for modulating protein elasticity through force-induced chemical transformations.