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Related Concept Videos

Peroxisomes01:24

Peroxisomes

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...
Peroxisomes and Mitochondria01:30

Peroxisomes and Mitochondria

Peroxisomes and mitochondria are two important oxygen-utilizing organelles in eukaryotic cells. Mitochondria carry out cellular respiration—the process that converts energy from food into ATP. Peroxisomes carry out a variety of functions, primarily breaking down different substances, such as fatty acids.
The peroxisome is a single membrane-bound cellular organelle that can perform several different functions, including lipid metabolism and chemical detoxification. The enzymes within peroxisomes...
Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

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 property is crucial in...
Radical Autoxidation01:20

Radical Autoxidation

The oxidation of an organic compound in the presence of air or oxygen is called autoxidation. For example, cumene reacts with oxygen to form hydroperoxide. Autoxidation involves initiation, propagation, and termination steps. Many organic compounds are susceptible to autoxidation—especially ethers in the presence of oxygen, which form hydroperoxides. Even though this reaction is slow, old ether bottles contain small amounts of peroxide, which leads to laboratory explosions during ether...
Redox Titration: Other Oxidizing and Reducing Agents01:26

Redox Titration: Other Oxidizing and Reducing Agents

Besides iodine, other oxidizing or reducing agents can serve as titrants in redox titrations. Common oxidizing titrants include KMnO4, cerium(IV), and K2Cr2O7. The choice of oxidizing titrants depends on factors like stability, cost, analyte strength, and reaction rate between the analyte and titrant. KMnO4 is a strong oxidizing titrant that reduces from Mn(VII) to Mn(II) in a highly acidic solution, simultaneously oxidizing the analyte to a higher oxidation state. In this case, KMnO4 acts as a...
Oxygen Requirements and Growth Patterns01:29

Oxygen Requirements and Growth Patterns

Microorganisms exhibit diverse oxygen requirements and growth patterns driven by their metabolic strategies and environmental adaptations. Oxygen, while essential for many organisms, can also be toxic under certain conditions, shaping how microorganisms grow and survive.Oxygen Requirements of MicroorganismsMicroorganisms are classified based on their ability to use or tolerate oxygen:● Obligate aerobes like Mycobacterium tuberculosis need oxygen for energy production, as it serves as the...

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Evaluating peroxiredoxin sensitivity toward inactivation by peroxide substrates.

Kimberly J Nelson1, Derek Parsonage, P Andrew Karplus

  • 1Department of Biochemistry, Wake Forest School of Medicine, Winston-Salem, North Carolina, USA.

Methods in Enzymology
|July 9, 2013
PubMed
Summary

Peroxiredoxins (Prxs) are enzymes that reduce peroxides but can be inactivated by them. This study introduces methods to quantify this sensitivity, aiding research on enzyme function and oxidative stress.

Keywords:
Cysteine sulfenic acidCysteine sulfinic acidHyperoxidationMass spectrometryOxidative inactivationPeroxidasePeroxide signalingRedox signaling

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Area of Science:

  • Biochemistry
  • Enzymology
  • Oxidative Stress Research

Background:

  • Peroxiredoxins (Prxs) are crucial antioxidant enzymes that reduce peroxides.
  • Prxs can undergo oxidative inactivation by their substrates, a process termed hyperoxidation.
  • The sensitivity to hyperoxidation varies among Prx enzymes and peroxide types, impacting their function.

Purpose of the Study:

  • To describe and validate methods for quantifying the sensitivity of Peroxiredoxins to oxidative inactivation.
  • To establish a standardized metric for comparing hyperoxidation sensitivity across different Prxs.
  • To investigate the physiological relevance of Prx hyperoxidation.

Main Methods:

  • Development and application of three distinct quantitative and semiquantitative assays.
  • Characterization of Prx sensitivity using various peroxide substrates.
  • Definition and utilization of the C(hyp1%) metric for sensitivity assessment.

Main Results:

  • Successful implementation of three distinct approaches to measure Prx hyperoxidation sensitivity.
  • Quantitative data obtained for Prx sensitivity under different conditions.
  • Introduction of C(hyp1%) as a comparable metric for hyperoxidation sensitivity.

Conclusions:

  • The described methods provide reliable means to quantify Peroxiredoxin sensitivity to hyperoxidation.
  • The C(hyp1%) metric offers a standardized and easily comparable measure for enzyme sensitivity.
  • Accurate quantification of Prx sensitivity is essential for understanding their physiological roles in oxidative stress response.