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Related Concept Videos

Pyruvate Oxidation01:15

Pyruvate Oxidation

After glycolysis, the charged pyruvate molecules enter the mitochondria via active transport and undergo three enzymatic reactions. These reactions ensure that pyruvate can enter the next metabolic pathway so that energy stored in the pyruvate molecules can be harnessed by the cells.
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...
Fermentation01:29

Fermentation

Most eukaryotic organisms require oxygen to survive and function adequately. Such organisms produce large amounts of energy during aerobic respiration by metabolizing glucose and oxygen into carbon dioxide and water. However, most eukaryotes can generate some energy in the absence of oxygen by anaerobic metabolism.
Fermentation is a type of metabolic process that occurs in the absence of oxygen, where organic molecules such as glucose are broken down to produce energy. During this process, the...
The Electron Transport Chain01:30

The Electron Transport Chain

The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q in...
Fates of Pyruvate01:20

Fates of Pyruvate

Pyruvate is the end product of glycolysis, where glucose is oxidized to pyruvate, simultaneously reducing NAD+ to NADH. Two molecules of ATP are also produced by substrate-level phosphorylation.
In aerobic organisms, pyruvate is metabolized via the citric acid cycle to produce reduced coenzymes NADH and FADH2. These coenzymes are then oxidized in the electron transport chain to produce ATP and, in the process, regenerate the NAD+ and FAD. As seen in some cell types and organisms, fermentation...
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...
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...

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Related Experiment Video

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

Published on: March 18, 2012

New quinoproteins in oxidative fermentation.

O Adachi1, D Moonmangmee, E Shinagawa

  • 1Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi 753-8515, Japan. osao@agr.yamaguchi-u.ac.jp

Biochimica Et Biophysica Acta
|April 11, 2003
PubMed
Summary

Newly identified quinoproteins in acetic acid bacteria offer versatile applications in oxidative fermentation for producing valuable compounds. These enzymes, including D-Arabitol dehydrogenase and meso-erythritol dehydrogenase, show promise for industrial applications like L-erythrulose and D-fructose synthesis.

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Area of Science:

  • Biochemistry
  • Microbiology
  • Enzymology

Background:

  • Acetic acid bacteria possess diverse quinoproteins with potential for biotechnological applications.
  • Oxidative fermentation using these enzymes enables the production of various useful materials.

Purpose of the Study:

  • To identify and characterize novel quinoproteins in acetic acid bacteria.
  • To explore the enzymatic capabilities of these quinoproteins for industrial applications.

Main Methods:

  • Purification of membrane-bound enzymes from bacterial strains.
  • Enzymatic assays to determine substrate specificity and reaction products.
  • Characterization of enzyme properties and catalytic activities.

Main Results:

  • D-Arabitol dehydrogenase catalyzes D-gluconate oxidation to 5-keto-D-gluconate.
  • A highly active membrane-bound cyclic alcohol dehydrogenase was purified from Gluconobacter frateurii.
  • Meso-erythritol dehydrogenase from G. frateurii CHM 43 effectively produces L-erythrulose.
  • Two distinct D-sorbitol dehydrogenases were identified, one producing D-fructose via irreversible oxidation.
  • Quinate dehydrogenase from various bacteria was purified and its activation by PQQ demonstrated.

Conclusions:

  • Newly identified quinoproteins in acetic acid bacteria demonstrate significant potential for fermentative production of valuable chemicals.
  • These enzymes offer advantages over existing methods, such as irreversible D-fructose synthesis.
  • Further research into quinoprotein function can unlock new biotechnological applications.