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Related Concept Videos

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...
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
Cofactors and Coenzymes01:27

Cofactors and Coenzymes

Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
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...
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...
Phase I Oxidative Reactions: Overview01:19

Phase I Oxidative Reactions: Overview

Phase I biotransformation, or functionalization, is a crucial chemical process that converts drugs and other xenobiotics into more water-soluble forms, facilitating expulsion from the body. It involves oxidative, reductive, and hydrolytic reactions that add or unveil polar functional groups on lipophilic substrates. Key players in phase I reactions are the mixed-function oxidases. Situated in liver cell microsomes, these enzymes predominantly carry out drug metabolism. They require molecular...

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Related Experiment Video

Updated: Jun 16, 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

Cofactor-independent oxidases and oxygenases.

Susanne Fetzner1, Roberto A Steiner

  • 1Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Münster, Germany. fetzner@uni-muenster.de

Applied Microbiology and Biotechnology
|February 17, 2010
PubMed
Summary

Cofactor-independent oxygenases and oxidases utilize unique catalytic mechanisms without metal ions or organic cofactors. These enzymes, including formylglycine-generating enzyme, offer potential for protein engineering and diverse biochemical applications.

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Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
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Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition

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Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
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Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

Related Experiment Videos

Last Updated: Jun 16, 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

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
08:31

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition

Published on: October 3, 2018

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

Area of Science:

  • Biochemistry
  • Enzymology
  • Protein Science

Background:

  • Most O(2)-metabolizing enzymes require metal ions or organic cofactors.
  • A subset of oxygenases and oxidases function without cofactors, presenting unique catalytic strategies.

Purpose of the Study:

  • To review and highlight the diverse group of cofactor-independent oxygenases and oxidases.
  • To discuss their mechanistic principles and potential applications.

Main Methods:

  • Literature review and analysis of known cofactor-independent enzymes.
  • Comparison of catalytic mechanisms and protein architectures.

Main Results:

  • Identified various cofactor-independent enzymes like urate oxidase, formylglycine-generating enzyme, PqqC, and specific bacterial oxygenases.
  • Highlighted that some enzymes, such as 3-hydroxy-4(1H)-quinolone 2,4-dioxygenases and Renilla luciferase, employ an alpha/beta-hydrolase fold.
  • Noted that these enzymes, despite diverse origins, may share a common mechanism involving substrate-assisted catalysis.

Conclusions:

  • Cofactor-independent enzymes represent a functionally diverse group with distinct evolutionary paths.
  • The shared principle of substrate-assisted catalysis offers insights into enzyme evolution and function.
  • Formylglycine-generating enzyme shows promise for protein engineering applications.