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Related Concept Videos

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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Oxidation of Alkenes: Anti Dihydroxylation with Peroxy Acids02:04

Oxidation of Alkenes: Anti Dihydroxylation with Peroxy Acids

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Diols are compounds with two hydroxyl groups. In addition to syn dihydroxylation, diols can also be synthesized through the process of anti dihydroxylation. The process involves treating an alkene with a peroxycarboxylic acid to form an epoxide. Epoxides are highly strained three-membered rings with oxygen and two carbons occupying the corners of an equilateral triangle. This step is followed by ring-opening of the epoxide in the presence of an aqueous acid to give a trans diol.
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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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Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide02:44

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Alkenes are converted to 1,2-diols or glycols through a process called dihydroxylation. It involves the addition of two hydroxyl groups across the double bond with two different stereochemical approaches, namely anti and syn. Dihydroxylation using osmium tetroxide progresses with syn stereochemistry.
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Peroxisomes and Mitochondria01:30

Peroxisomes and Mitochondria

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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...
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Oxidation of Alkenes: Syn Dihydroxylation with Potassium Permanganate02:21

Oxidation of Alkenes: Syn Dihydroxylation with Potassium Permanganate

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Alkenes can be dihydroxylated using potassium permanganate.  The method encompasses the reaction of an alkene with a cold, dilute solution of potassium permanganate under basic conditions to form a cis-diol along with a brown precipitate of manganese dioxide.
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Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
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DyP-Type Peroxidases: Recent Advances and Perspectives.

Yasushi Sugano1, Toru Yoshida1

  • 1Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University, Tokyo 112-8681, Japan.

International Journal of Molecular Sciences
|June 2, 2021
PubMed
Summary

The DyP-type peroxidase family, found in bacteria and fungi, shows diverse structures and functions beyond simple peroxidase activity. Research highlights their unique roles in iron transport and lignin degradation.

Keywords:
DyPDyP-type peroxidaseantifungal anthraquinone compoundscargo proteinencapsulinhydrolaseiron uptakelife cyclelignin degradationnano compartmentoxidasestructure-based sequence alignments

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Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • DyP-type peroxidases are a diverse enzyme family primarily found in bacteria and fungi.
  • Recent research has uncovered their widespread distribution and varied structural features.

Purpose of the Study:

  • To review research progress on DyP-type peroxidases over the past decade.
  • To highlight their structural diversity, catalytic mechanisms, and diverse physiological roles.

Main Methods:

  • Tertiary structural analyses of DyP-type peroxidases.
  • Review of literature on their enzymatic activities and cellular functions.
  • Comparison with other heme peroxidases.

Main Results:

  • DyP-type peroxidases exhibit unique catalytic cycles distinct from other heme peroxidases.
  • They possess additional hydrolase or oxidase activities and varied cellular localization.
  • Key roles identified in Streptomyces life-cycle switching and iron transport systems in bacteria.

Conclusions:

  • The DyP-type peroxidase family is a rich source of diverse enzymes with significant research potential.
  • Their functions extend beyond lignin degradation, including environmental roles like degrading anthraquinones.