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Redox Equilibria: Overview01:23

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A reduction-oxidation reaction is commonly called a redox reaction. In a redox reaction, electrons are transferred from one species to another rather than being shared between or among atoms. The reducing agent or reductant is the species that loses electrons and gets oxidized in the process. The species that gains electrons and gets reduced in the process is the oxidizing agent or oxidant. Redox reactions are represented as two separate equations called half-reactions, where one equation...
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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...
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Electrochemistry is the science involved in the interconversion of electrical and chemical reactions. Such reactions are called reduction-oxidation, or redox reactions. These important reactions are defined by changes in oxidation states for one or more reactant elements and include a subset of reactions involving the transfer of electrons between reactant species. Electrochemistry as a field has evolved to yield sufficient insights on the fundamental principles of redox chemistry and multiple...
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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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Ladder diagrams are useful tools for understanding redox equilibrium reactions, especially the effects of concentration changes on the electrochemical potential of the reaction. The vertical axis in the redox ladder diagrams represents the electrochemical potential, E. The area of predominance is demarcated using the Nernst equation.
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Computational modeling of redox enzymes.

Per E M Siegbahn1

  • 1Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Sweden.

FEBS Letters
|October 18, 2022
PubMed
Summary

This study presents a computational method using hybrid density functional theory to accurately model redox-active enzymes. Calculations on photosystem II and nitrogenase offer insights into water oxidation and nitrogen activation mechanisms.

Keywords:
hybrid density functional theorymechanismsnitrogenasephotosystem IIredox enzymes

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Area of Science:

  • Computational chemistry
  • Biochemistry
  • Enzyme mechanisms

Background:

  • Redox-active enzymes play crucial roles in biological processes.
  • Accurately modeling enzyme mechanisms is essential for understanding their function.
  • Hybrid density functional theory (DFT) offers a promising approach for such modeling.

Purpose of the Study:

  • To describe a computational methodology for accurately modeling redox-active enzyme mechanisms.
  • To apply this methodology to key biological processes: water oxidation in photosystem II and N2 activation by nitrogenase.

Main Methods:

  • Utilizing hybrid density functional theory (DFT).
  • Incorporating a fraction of exact exchange within the DFT framework.
  • Applying the methodology to analyze the mechanisms of photosystem II and nitrogenase.

Main Results:

  • The computational method accurately describes enzyme mechanisms.
  • For photosystem II, the calculated water oxidation mechanism is strongly supported by experimental data.
  • For nitrogenase, calculations suggest a pre-catalytic activation step, which is currently debated.

Conclusions:

  • The developed hybrid DFT methodology is effective for studying redox-active enzyme mechanisms.
  • The findings provide strong support for the proposed mechanism in photosystem II.
  • The study highlights a potential pre-catalytic activation step in nitrogenase, warranting further investigation.