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Related Concept Videos

Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
Role of Reduced Coenzymes NADH and FADH₂01:29

Role of Reduced Coenzymes NADH and FADH₂

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...
Electron Transport Chains01:28

Electron Transport Chains

The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
The ETC is comprised of...
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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...
Cofactors and Coenzymes01:24

Cofactors and Coenzymes

Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...

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Updated: Jun 19, 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

Flavin-containing heme enzymes.

Christopher G Mowat1, Ben Gazur, Laura P Campbell

  • 1EaStCHEM School of Chemistry, University of Edinburgh, West Mains Road, Edinburgh EH9 3JJ, UK. C.G.Mowat@ed.ac.uk

Archives of Biochemistry and Biophysics
|October 24, 2009
PubMed
Summary
This summary is machine-generated.

Oxidative enzymes with flavin and heme groups are crucial. This article reviews five such enzymes, detailing their structures, mechanisms, and electron transfer for substrate oxidation.

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Light-driven Enzymatic Decarboxylation
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Light-driven Enzymatic Decarboxylation

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Last Updated: Jun 19, 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

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

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Light-driven Enzymatic Decarboxylation
09:58

Light-driven Enzymatic Decarboxylation

Published on: May 22, 2016

Area of Science:

  • Biochemistry
  • Enzymology
  • Bioinorganic Chemistry

Background:

  • Oxidative enzymes often utilize flavin and heme prosthetic groups.
  • These enzymes play vital roles in various biological oxidation reactions.

Purpose of the Study:

  • To review five key oxidative enzymes containing both flavin and heme cofactors.
  • To discuss their structures, catalytic mechanisms, and electron transfer processes.

Main Methods:

  • Comparative analysis of enzyme structures.
  • Review of catalytic mechanisms and electron transfer pathways.
  • Focus on L-lactate dehydrogenase flavocytochrome b(2), cellobiose dehydrogenase, flavohemoglobin, nitric oxide synthase, and flavocytochrome P450 BM3.

Main Results:

  • Two enzymes (L-lactate dehydrogenase flavocytochrome b(2), cellobiose dehydrogenase) catalyze reactions at the flavin site.
  • Three enzymes (flavohemoglobin, nitric oxide synthase, flavocytochrome P450 BM3) activate dioxygen at the heme site.
  • Some enzymes share significant structural homology despite diverse functions.

Conclusions:

  • Flavin-heme enzymes exhibit diverse mechanisms for substrate oxidation.
  • Understanding electron transfer between cofactors is key to their function.
  • Recent advances provide new insights into these fascinating enzyme systems.