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Hydrogen Bonds00:26

Hydrogen Bonds

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Hydrogen bonds are weak attractions between atoms that have formed other chemical bonds. One of these atoms is electronegative, like oxygen, and has a partial negative charge. The other is a hydrogen atom that has bonded with another electronegative atom and has a partial positive charge.
Hydrogen Bonds Control the World!
Because hydrogen has very weak electronegativity when it binds with a strongly electronegative atom, such as oxygen or nitrogen, electrons in the bond are unequally shared....
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Hydrogen Bonds01:04

Hydrogen Bonds

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A hydrogen bond is formed when a weakly positive hydrogen atom already bonded to one electronegative atom (for example, the oxygen in the water molecule) is attracted to another electronegative atom from another polar molecule, such as water (H2O), hydrogen fluoride (HF), or ammonia (NH3). The huge electronegativity difference between the H atom (2.1) and the atom to which it is bonded (4.0 for an F atom, 3.5 for an O atom, or 3.0 for an N atom), combined with the very small size of an H atom...
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Autoxidation of Ethers to Peroxides and Hydroperoxides02:23

Autoxidation of Ethers to Peroxides and Hydroperoxides

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Ethers represent a class of chemical compounds that become more dangerous with prolonged storage because they tend to form explosive peroxides when standing in the air. Autoxidation is the spontaneous oxidation of a compound in air. In the presence of oxygen, ethers slowly oxidize to form hydroperoxides and dialkyl peroxides.
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Regioselectivity of Electrophilic Additions-Peroxide Effect02:35

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In the presence of organic peroxides, the addition of hydrogen bromide to an alkene yields the isomer that is not predicted by Markovnikov’s rule. For example, the addition of hydrogen bromide to 2-methylpropene in the presence of peroxides gives 1-bromo-2-methylpropane. This addition reaction proceeds via a free radical mechanism, which reverses the regioselectivity. The free radical reaction mechanism involves three stages: initiation, propagation, and termination.
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Functional Groups02:45

Functional Groups

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Functional groups are a group of atoms with characteristic properties, which when linked to the carbon skeleton of a molecule, alter the properties of that molecule. For example, the presence of certain functional groups on a molecule will make them hydrophilic, whereas others will make them hydrophobic. These functional groups are an indispensable part of organic chemistry and important components of biological molecules, such as carbohydrates, proteins, lipids, and nucleic acids. Each...
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Reduction of Alkenes: Catalytic Hydrogenation02:13

Reduction of Alkenes: Catalytic Hydrogenation

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Alkenes undergo reduction by the addition of molecular hydrogen to give alkanes. Because the process generally occurs in the presence of a transition-metal catalyst, the reaction is called catalytic hydrogenation.
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The hydrogenation process takes place on the...
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Bioluminescence Imaging of NADPH Oxidase Activity in Different Animal Models
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Bioluminescence Imaging of NADPH Oxidase Activity in Different Animal Models

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NADPH oxidase 4 function as a hydrogen peroxide sensor.

Yukio Nisimoto1, Hisamitsu Ogawa2, Yuzo Kadokawa2

  • 1Department of Biomedical Science, College of Life and Health Science, Chubu University, 1200 Matsumoto-cho, Kasugai, Aichi 487-8501, Japan.

Journal of Biochemistry
|January 25, 2018
PubMed
Summary
This summary is machine-generated.

Nox4 (NADPH oxidase 4) activity is regulated by its dehydrogenase domain, with specific cysteine mutations significantly reducing reactive oxygen species (ROS) production and impacting enzyme function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Physiology

Background:

  • Nox4, a constitutively active enzyme, generates reactive oxygen species (ROS) and is implicated in various cellular processes.
  • Understanding Nox4 regulation is crucial for elucidating its role in health and disease.

Purpose of the Study:

  • To investigate the role of the Nox4 dehydrogenase (DH) domain in enzyme activity and regulation.
  • To identify specific mutations affecting Nox4 oxidase activity and ROS production.

Main Methods:

  • HEK293 cells were transfected with His6-tagged Nox4 to study its expression and interaction with p22phox.
  • Nucleus-enriched fractions (NEF) were analyzed for NADPH oxidation rates.
  • Site-directed mutagenesis was used to create Nox4 mutants (P437H, C546S, C546L, C547L) to assess their oxidase activity and ROS production.

Main Results:

  • Nox4 expression increased p22phox levels and heterodimer formation in HEK293 cells.
  • Nox4(P437H) mutant exhibited almost complete loss of oxidase activity, while cysteine mutants (C546S, C546L, C547L) significantly reduced ROS production.
  • Conserved cysteine residues (C546, C547) in the DH domain are critical for regulating Nox4 activity in response to H2O2 concentration.

Conclusions:

  • The dehydrogenase domain of Nox4 plays a key role in its catalytic activity and regulation.
  • Specific cysteine residues within the DH domain are essential for Nox4-mediated ROS generation and are sensitive to cellular H2O2 levels.