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Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

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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.
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Besides iodine, other oxidizing or reducing agents can serve as titrants in redox titrations. Common oxidizing titrants include KMnO4, cerium(IV), and K2Cr2O7. The choice of oxidizing titrants depends on factors like stability, cost, analyte strength, and reaction rate between the analyte and titrant. KMnO4 is a strong oxidizing titrant that reduces from Mn(VII) to Mn(II) in a highly acidic solution, simultaneously oxidizing the analyte to a higher oxidation state. In this case, KMnO4 acts as a...
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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.
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In this lesson, the oxidation of alcohols is discussed in depth. The various reagents used for oxidation of primary and secondary alcohols are detailed, and their mechanism of action is provided.
The process of oxidation in a chemical reaction is observed in any of the three forms:
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Light-driven Enzymatic Decarboxylation
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An unprecedented function for a tungsten-containing oxidoreductase.

Liju G Mathew1, Dominik K Haja1, Clayton Pritchett1

  • 1Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, 30602, USA.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|October 21, 2022
PubMed
Summary

Researchers identified the fifth tungstopterin enzyme in Pyrococcus furiosus, named aliphatic sulfonate ferredoxin oxidoreductase (ASOR). This enzyme, crucial during cold shock, oxidizes aliphatic sulfonates and has a unique heterodimeric structure.

Keywords:
Aliphatic sulfonatesCold response proteinCrystal structurePyrococcus furiosusTaurineTungstoenzymeWOR5

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Extremophile Research

Background:

  • Pyrococcus furiosus possesses five tungstopterin-containing oxidoreductases with diverse aldehyde oxidation roles.
  • The function of the fifth enzyme, WOR5, remained unknown despite its increased expression during cold shock (72°C).

Purpose of the Study:

  • To elucidate the structure and identify the physiological substrate of WOR5 from Pyrococcus furiosus.
  • To understand the role of WOR5 in the organism's response to cold shock.

Main Methods:

  • Crystallization of WOR5 from a cytoplasmic extract of P. furiosus grown at 72°C.
  • Deduction of the enzyme's structure using X-ray crystallography.
  • Biochemical assays and product analysis to determine substrate specificity.

Main Results:

  • WOR5 was determined to be a heterodimer with a polyferredoxin-like subunit containing [4Fe-4S] clusters.
  • The active site structure differs significantly from related enzymes AOR and FOR.
  • WOR5 was identified as aliphatic sulfonate ferredoxin oxidoreductase (ASOR), catalyzing aliphatic sulfonate oxidation.

Conclusions:

  • ASOR possesses a unique structure and function among P. furiosus tungstopterin enzymes.
  • The proposed catalytic mechanism provides insights into its biochemical activity.
  • ASOR likely plays a role in the cold-shock response pathway in this hyperthermophile.