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Related Concept Videos

Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

7.8K
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.
7.8K
Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

5.1K
In the presence of oxidizing agents, phenols are oxidized to quinones. Quinones can be easily reduced back to phenols using mild reducing agents. The electron-donating hydroxyl group enhances the reactivity of the aromatic ring, enabling oxidation of the ring even in the absence of an α hydrogen.
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox...
5.1K
Hemoglobin01:24

Hemoglobin

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Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
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Sulfur Assimilation01:20

Sulfur Assimilation

477
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...
477
Oxidation of Alcohols02:37

Oxidation of Alcohols

17.6K
In this lesson, the oxidation of alcohols is discussed in depth. The various reagents used for oxidation of primary and secondary alcohols are detailed, and their mechanism of action is provided.
The process of oxidation in a chemical reaction is observed in any of the three forms:
17.6K
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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Related Experiment Video

Updated: Mar 18, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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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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Thiol-induced hemoglobin oxidation.

V Lips1, G Celedón1, J Escobar2

  • 1a Departamento de Fisiología, Facultad de Ciencias , Universidad de Valparaiso.

Redox Report : Communications in Free Radical Research
|July 14, 2016
PubMed
Summary
This summary is machine-generated.

Cysteine addition oxidizes oxyhemoglobin and destroys its sulfhydryl groups. This reaction, involving superoxide and hydrogen peroxide, is accelerated by hemoprotein catalysis, impacting red blood cells.

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Measurement of Heme Synthesis Levels in Mammalian Cells
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Area of Science:

  • Biochemistry
  • Redox Biology

Background:

  • Oxyhemoglobin is crucial for oxygen transport.
  • The role of thiol compounds like cysteine in oxyhemoglobin stability is not fully understood.

Purpose of the Study:

  • To investigate the oxidation of oxyhemoglobin by cysteine.
  • To elucidate the mechanism and factors influencing this reaction.

Main Methods:

  • Incubation of purified oxyhemoglobin, red blood cell lysate, and suspensions with cysteine.
  • Monitoring hemoprotein oxidation and sulfhydryl group destruction.
  • Assessing the effects of catalase and sodium azide.

Main Results:

  • Cysteine (mM range) caused significant oxyhemoglobin oxidation and sulfhydryl group destruction.
  • The reaction rate depended on initial concentrations and was limited by thiol depletion.
  • Oxidation was faster in purified oxyhemoglobin than in lysate due to catalase inhibition.
  • Superoxide anion and hydrogen peroxide were implicated in the mechanism.
  • A chain oxidation mechanism explained extensive cysteine destruction.

Conclusions:

  • Cysteine readily oxidizes oxyhemoglobin, leading to hemoprotein damage.
  • The reaction involves reactive oxygen species and is influenced by cellular components like catalase.
  • Understanding these redox interactions is vital for hemoglobin stability and red blood cell function.