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Related Concept Videos

Corrosion02:49

Corrosion

The degradation of metals due to natural electrochemical processes is known as corrosion. Rust formation on iron, tarnishing of silver, and the blue-green patina that develops on copper are examples of corrosion. Corrosion involves the oxidation of metals. Sometimes it is protective, such as the oxidation of copper or aluminum, wherein a protective layer of metal oxide or its derivatives forms on the surface, protecting the underlying metal from further oxidation. In other cases, corrosion is...
Redox Reactions01:24

Redox Reactions

Oxidation-reduction or redox reactions involve the transfer of electrons from one molecule or atom to another. When an atom gains an electron, another atom must lose an electron, meaning oxidation and reduction must occur together. Since the redox occurs in pairs, the atom that gets oxidized is also called the reducing agent or reductant, and the atom that is reduced is also called the oxidizing agent or oxidant. A straightforward way to remember the definitions of oxidation and reduction is...
Redox Reactions01:27

Redox Reactions

Redox reactions are vital biochemical processes that underpin energy metabolism in cells. These reactions involve the transfer of electrons between molecules, occurring in tandem as oxidation and reduction. Oxidation refers to the loss of electrons, while reduction denotes their gain. This coupling ensures the seamless flow of electrons through metabolic pathways. For example, in bacterial metabolism, glucose undergoes oxidation to carbon dioxide, while oxygen is simultaneously reduced to...
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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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Oxidation–Reduction Reactions
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A reduction-oxidation reaction is commonly called a redox reaction. In a redox reaction, electrons are transferred from one species to another rather than being shared between or among atoms. The reducing agent or reductant is the species that loses electrons and gets oxidized in the process. The species that gains electrons and gets reduced in the process is the oxidizing agent or oxidant. Redox reactions are represented as two separate equations called half-reactions, where one equation...

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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-based redox signalling: rust never sleeps.

Merridee A Wouters1, Siiri Iismaa, Samuel W Fan

  • 1Deakin University, Geelong 3217, Vic, Australia. m.wouters@deakin.edu.au

The International Journal of Biochemistry & Cell Biology
|April 26, 2011
PubMed
Summary
This summary is machine-generated.

Protein cysteine modifications, including oxidation and nitrosation, alter protein structures and trigger biological signals. Understanding these structural changes reveals mechanisms of cellular signaling pathways.

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cellular Signaling

Background:

  • Cysteine residues in proteins are targets for modification during oxidative and nitrosative stress.
  • These modifications include oxidation, nitrosation, glutathionylation, and disulfide bond formation.
  • Such modifications play crucial roles in cellular signaling pathways.

Purpose of the Study:

  • To elucidate the mechanistic aspects of signaling pathways involving modified cysteines.
  • To understand how cysteine modifications induce conformational changes in proteins.
  • To correlate structural changes with biological responses.

Main Methods:

  • Analysis of protein structures with modified cysteines.
  • Investigating conformational changes upon specific modifications like nitric oxide and glutathione conjugation.
  • Examining structural alterations resulting from disulfide bond formation and reduction.

Main Results:

  • Conformational changes upon nitric oxide and glutathione conjugation are typically small, often increasing local protein disorder.
  • Burial of nitric oxide can extend the duration of signaling.
  • Disulfide formation/reduction can lead to significant structural changes, including order/disorder transitions, metal expulsion, major backbone reorganization, and quaternary structure alterations like domain swapping.

Conclusions:

  • Structural insights into modified cysteines are crucial for understanding signaling mechanisms.
  • The nature and extent of conformational changes vary significantly depending on the type of cysteine modification.
  • These structural dynamics are fundamental to how cells respond to stress and regulate biological processes.