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Redox Reactions01:24

Redox Reactions

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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...
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Redox Reactions01:27

Redox Reactions

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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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Peroxisomes01:24

Peroxisomes

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Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
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Peroxisomes01:24

Peroxisomes

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Redox Equilibria: Overview01:23

Redox Equilibria: Overview

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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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Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

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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...
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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
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Peroxiredoxin Catalysis at Atomic Resolution.

Arden Perkins1, Derek Parsonage2, Kimberly J Nelson2

  • 1Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, USA.

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|September 6, 2016
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Summary
This summary is machine-generated.

Peroxiredoxins (Prxs) protect cells from oxidative damage. Structural analysis reveals how PrxQ enzyme unfolding enhances catalysis and how crystal contacts can lead to inactivation, informing drug target strategies.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Peroxiredoxins (Prxs) are crucial cysteine-based peroxidases involved in cellular redox regulation and pathogen virulence.
  • Understanding their catalytic mechanism and susceptibility to oxidative damage is vital for biological and therapeutic applications.

Purpose of the Study:

  • To elucidate the reaction pathway of a PrxQ subfamily enzyme from Xanthomonas campestris at atomic resolution.
  • To investigate the role of active site conformation in Prx catalysis and hyperoxidation.

Main Methods:

  • Analysis of catalytically active crystals of a PrxQ enzyme.
  • Determination of atomic resolution structures capturing key catalytic intermediates (thiolate, sulfenate, sulfinate).

Main Results:

  • High-resolution structures revealed non-standard sulfenate intermediate geometry, suggesting local unfolding enhances catalysis.
  • Crystal contacts preventing unfolding led to facile hyperoxidative inactivation, even in resistant Prxs.
  • Structures provide accurate data for theoretical studies and mechanistic insights.

Conclusions:

  • Sulfenate formation can induce active site unfolding, promoting efficient catalysis in PrxQ enzymes.
  • Conformation-specific inhibition strategies may be effective for targeting Prxs, particularly drug-resistant variants.