Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

4.5K
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...
4.5K
Oxidation and Reduction of Organic Molecules01:19

Oxidation and Reduction of Organic Molecules

8.0K
Energy production within a cell involves many coordinated chemical pathways. Most of these pathways are combinations of oxidation and reduction reactions, which occur at the same time. An oxidation reaction strips an electron from an atom in a compound, and the addition of this electron to another compound is a reduction reaction. Because oxidation and reduction usually occur together, these pairs of reactions are called redox reactions.
The removal of an electron from a molecule, results in a...
8.0K
Redox Reactions01:27

Redox Reactions

1.2K
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...
1.2K
Redox Reactions01:24

Redox Reactions

50.9K
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...
50.9K
Role of Reduced Coenzymes NADH and FADH₂01:29

Role of Reduced Coenzymes NADH and FADH₂

11.8K
The energy released from the breakdown of the chemical bonds within nutrients can be stored either through the reduction of electron carriers or in the bonds of adenosine triphosphate (ATP). In living systems, a small class of compounds functions as mobile electron carriers, molecules that bind to and shuttle high-energy electrons between compounds in pathways. The principal electron carriers that will be considered originate from the B vitamin group and are derivatives of nucleotides; they are...
11.8K
Oxidation-Reduction Reactions03:11

Oxidation-Reduction Reactions

58.6K
Oxidation–Reduction Reactions
58.6K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Targeting a Unique Cysteine Residue to Achieve Isoform-Selective Inhibition of the Proline Biosynthetic Enzyme Pyrroline-5-Carboxylate Reductase 2.

ACS chemical biology·2026
Same author

Crystallographic Fragment Screening of a Bifunctional Proline Catabolic Enzyme Reveals New Inhibitor Templates for Proline Dehydrogenase and L-Glutamate-γ-semialdehyde Dehydrogenase.

Molecules (Basel, Switzerland)·2024
Same author

Noncovalent Inhibition and Covalent Inactivation of Proline Dehydrogenase by Analogs of <i>N</i>-Propargylglycine.

Biochemistry·2024
Same author

Screening a knowledge-based library of low molecular weight compounds against the proline biosynthetic enzyme 1-pyrroline-5-carboxylate 1 (PYCR1).

Protein science : a publication of the Protein Society·2024
Same author

Novel Fragment Inhibitors of PYCR1 from Docking-Guided X-ray Crystallography.

Journal of chemical information and modeling·2024
Same author

Structural and functional analysis of two SHMT8 variants associated with soybean cyst nematode resistance.

The FEBS journal·2023
Same journal

Aromatic Cage-Directed Azide-Methyllysine Photochemistry for Profiling Nonhistone Interacting Partners of the MeCP2 Methyl-CpG-Binding Domain.

Biochemistry·2026
Same journal

Differential Hydroxypyruvate Processing by <i>E. coli</i> and <i>P. aeruginosa</i> DXP Synthases Reveals Preferential Xylulose 5-Phosphate Formation by the <i>P. aeruginosa</i> Enzyme.

Biochemistry·2026
Same journal

Structural and Functional Characterization of Heterologous Nitrogenase Complexes.

Biochemistry·2026
Same journal

Discovery of Bacterial Unspecific Peroxygenases.

Biochemistry·2026
Same journal

Lactate Biology: Subcellular Routing and Chemical Form Define Function.

Biochemistry·2026
Same journal

Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.

Biochemistry·2026
See all related articles

Related Experiment Video

Updated: Apr 28, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
12:08

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry

Published on: March 18, 2012

17.6K

Structural Principles of Covalent Flavin Modification in Oxidoreductases.

John J Tanner1

  • 1Departments of Biochemistry and Chemistry, University of Missouri, Columbia, Missouri 65211, United States.

Biochemistry
|April 27, 2026
PubMed
Summary
This summary is machine-generated.

Flavin-dependent enzymes can be irreversibly inactivated by covalent modification of their flavin cofactor. This review highlights structural data revealing common modification sites and enzyme classes prone to inactivation, particularly amine oxidases.

Keywords:
X-ray crystallographycovalent inhibitioncovalent modificationflavoenzymes

More Related Videos

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
08:57

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

9.3K
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.7K

Related Experiment Videos

Last Updated: Apr 28, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
12:08

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry

Published on: March 18, 2012

17.6K
Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
08:57

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

9.3K
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.7K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Flavin-dependent oxidoreductases utilize the versatile isoalloxazine cofactor for diverse biochemical reactions.
  • The N5 and C4a atoms of flavin are crucial for catalysis and can undergo covalent modification.
  • Covalent modification can lead to enzyme inactivation, impacting biological processes.

Purpose of the Study:

  • To review structurally validated examples of covalent flavin inactivation in enzymes.
  • To identify common structural outcomes and enzyme families susceptible to covalent modification.
  • To explore the mechanistic basis and distribution of covalent flavin inactivation.

Main Methods:

  • Analysis of X-ray crystallography data from the Protein Data Bank.
  • Review of literature on flavoenzyme inactivation mechanisms.
  • Integration of structural, mechanistic, and inhibitor design perspectives.

Main Results:

  • Covalent flavin modification occurs in multiple enzyme families, including monoamine oxidases and dehydrogenases.
  • Common outcomes include N5 or C4a alkylation, flavin reduction, and ring distortion.
  • Amine oxidases and dehydrogenases are frequently inactivated due to iminium intermediate formation during C-N bond oxidation.

Conclusions:

  • The structural record reveals recurring patterns in covalent flavin inactivation.
  • Mechanistic features of certain enzyme classes predispose them to irreversible flavin modification.
  • Understanding these mechanisms informs enzyme function studies and inhibitor design.