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Related Concept Videos

Radical Reactivity: Overview01:11

Radical Reactivity: Overview

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Radicals, the highly reactive species, gain stability by undergoing three different reactions. The first reaction involves a radical-radical coupling, in which a radical combines with another radical, forming a spin‐paired molecule. The second reaction is between a radical and a spin‐paired molecule, generating a new radical and a new spin‐paired molecule. The third reaction is radical decomposition in a unimolecular reaction, forming a new radical and a spin‐paired...
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Radical Formation: Addition00:47

Radical Formation: Addition

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Radicals can be formed by adding a radical to a spin-paired molecule. This is typically observed with unsaturated species, where the addition of a radical across the π bond leads to the production of a new radical by dissolving the π bond. For example, the addition of a Br radical to an alkene yields a carbon-centered radical.
Similar to charge conservation in chemical reactions, spin conservation is implicit for radical reactions. Accordingly, the product formed must possess an...
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Radical Formation: Overview01:03

Radical Formation: Overview

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A bond can be broken either by heterolytic bond cleavage to form ions or homolytic bond cleavage to yield radicals. A fishhook arrow is used to represent the motion of a single electron in homolytic bond cleavage. There are two main sources from which radicals can be formed:
Radicals from spin-paired molecules:
Radicals can be obtained from spin-paired molecules either by homolysis or electron transfer. While two radicals are formed in the former, an electron is added in the...
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Ribozymes02:47

Ribozymes

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The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can...
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Radicals: Electronic Structure and Geometry01:07

Radicals: Electronic Structure and Geometry

4.1K
This lesson delves into the geometry of a radical, which is influenced by the electronic structure of the molecule. The principle is similar to that of a lone pair, where the unpaired electron influences the geometry at the radical center.
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Radical Reactivity: Intramolecular vs Intermolecular01:33

Radical Reactivity: Intramolecular vs Intermolecular

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Radical reactions can occur either intermolecularly or intramolecularly. In an intermolecular radical reaction, a nucleophilic radical adds to an electrophilic alkene or vice versa. In such reactions, the radical and generally the alkene, which is also called the radical trap, are two different molecules. Additionally, for such intermolecular reactions to occur, the radical trap must be active, present in an excess concentration, and the radical starting material must have a weak...
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Monitoring Equilibrium Changes in RNA Structure by 'Peroxidative' and 'Oxidative' Hydroxyl Radical Footprinting
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Structure of a ribonucleotide reductase R2 protein radical.

Hugo Lebrette1,2, Vivek Srinivas1, Juliane John1

  • 1Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Stockholm, Sweden.

Science (New York, N.Y.)
|October 5, 2023
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Aerobic ribonucleotide reductases (RNRs) generate a radical in R2 to build DNA. A new structure shows how RNR shields and moves this radical for DNA synthesis via proton-coupled electron transfer (PCET).

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Aerobic ribonucleotide reductases (RNRs) are essential enzymes for DNA synthesis.
  • RNRs generate a critical free radical in the R2 subunit for catalysis.
  • Radical transfer to the R1 subunit occurs via proton-coupled electron transfer (PCET).

Purpose of the Study:

  • To determine the high-resolution structure of the class Ie R2 protein radical.
  • To elucidate the mechanism of radical shielding and translocation within RNR.
  • To understand the structural basis of radical transfer during PCET.

Main Methods:

  • X-ray free electron laser serial femtosecond crystallography (XFEL-SFX) at room temperature.
  • High-resolution structural analysis of the R2 protein radical.

Main Results:

  • Revealed conformational changes in R2 that shield the radical.
  • Identified structural rearrangements connecting the radical to the translocation path.
  • Observed restructuring of the hydrogen bond network, including a short O-O bond (2.41 Å), potentially gating radical transfer.

Conclusions:

  • The structure explains how RNR handles and mobilizes the radical for PCET.
  • Structural insights provide a basis for understanding radical transfer mechanisms in proteins.
  • Findings have implications for the broader field of radical chemistry in biological systems.