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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...
Peroxisomes01:30

Peroxisomes

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...
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...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:

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Related Experiment Video

Updated: Jul 8, 2026

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples
05:17

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples

Published on: July 28, 2016

Chloroperoxidase, a janus enzyme.

Kelath Murali Manoj1, Lowell P Hager

  • 1Department of Biochemistry, University of Illinois at Urbana-Champaign, 6000 South Mathews Avenue, Urbana, Illinois 61801, USA. satyamjayatu@yahoo.com

Biochemistry
|January 29, 2008
PubMed
Summary

Chloroperoxidase catalyzes distinct one-electron and two-electron oxidations. Alkylation revealed that one-electron reactions are unaffected, while two-electron reactions are inhibited, suggesting different mechanisms and substrate interactions.

Area of Science:

  • Biochemistry
  • Enzymology
  • Fungal Metabolism

Background:

  • Chloroperoxidase is a fungal heme-thiolate enzyme known for catalyzing diverse oxidation reactions.
  • Understanding the distinct mechanisms of one-electron and two-electron oxidations is crucial for enzyme function.

Purpose of the Study:

  • To investigate the mechanistic differences between one-electron and two-electron oxidations catalyzed by chloroperoxidase.
  • To elucidate the role of an essential histidine residue and substrate interaction sites in chloroperoxidase activity.

Main Methods:

  • Enzyme alkylation targeting a key histidine residue.
  • Analysis of pH-dependent activity profiles for various peroxidative substrates.
  • Characterization of substrate conversion rates with different activators (hydrogen peroxide vs. alkylhydroperoxides).

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Imaging of mtHyPer7, a Ratiometric Biosensor for Mitochondrial Peroxide, in Living Yeast Cells
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Imaging of mtHyPer7, a Ratiometric Biosensor for Mitochondrial Peroxide, in Living Yeast Cells

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Last Updated: Jul 8, 2026

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples
05:17

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples

Published on: July 28, 2016

Peroxisome Staining in Mammalian Cells Using Peroxisome-Specific Probes
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Peroxisome Staining in Mammalian Cells Using Peroxisome-Specific Probes

Published on: December 19, 2025

Imaging of mtHyPer7, a Ratiometric Biosensor for Mitochondrial Peroxide, in Living Yeast Cells
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Imaging of mtHyPer7, a Ratiometric Biosensor for Mitochondrial Peroxide, in Living Yeast Cells

Published on: June 2, 2023

Main Results:

  • Alkylation of the essential histidine residue inhibited two-electron oxidations but not one-electron oxidations.
  • Optimal pH varied for different substrates undergoing peroxidation.
  • Substrates unable to access the active site were efficiently converted, suggesting peripheral interactions.
  • Small alkylhydroperoxides were superior activators for peroxidation compared to hydrogen peroxide.

Conclusions:

  • One-electron and two-electron oxidations catalyzed by chloroperoxidase exhibit distinct mechanisms.
  • Substrate interaction likely occurs outside the heme active site, potentially at the enzyme's surface.
  • The essential histidine residue plays a critical role specifically in two-electron oxidation pathways.