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Related Concept Videos

Redox Reactions01:27

Redox Reactions

Redox reactions are vital biochemical processes that underpin energy metabolism in cells. These reactions involve the transfer of electrons between molecules, occurring in tandem as oxidation and reduction. Oxidation refers to the loss of electrons, while reduction denotes their gain. This coupling ensures the seamless flow of electrons through metabolic pathways. For example, in bacterial metabolism, glucose undergoes oxidation to carbon dioxide, while oxygen is simultaneously reduced to...
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Transcriptional Regulation: Riboswitches

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Related Experiment Video

Updated: Jun 22, 2026

EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1
06:01

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Published on: November 26, 2014

Redox-linked structural changes in ribonucleotide reductase.

A R Offenbacher1, I R Vassiliev, M R Seyedsayamdost

  • 1Department of Chemistry and Biochemistry and the Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.

Journal of the American Chemical Society
|June 4, 2009
PubMed
Summary
This summary is machine-generated.

Ribonucleotide reductase (RNR) uses a tyrosyl radical (Y122*) to initiate catalysis. This study reveals redox-linked structural changes in nearby amide bonds, driven by electrostatic shifts in the radical

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Spectroscopy

Background:

  • Ribonucleotide reductase (RNR) is essential for DNA synthesis, catalyzing deoxyribonucleotide production.
  • Class I RNRs, like the E. coli beta2 subunit, feature iron centers and a critical tyrosyl free radical (Y122*) for catalysis.
  • Redox-dependent conformational changes in Y122* may regulate proton-coupled electron transfer.

Purpose of the Study:

  • To investigate redox-linked structural changes associated with the Y122* radical in E. coli beta2.
  • To understand the role of the tyrosyl radical in initiating catalytic reactions.
  • To explore the mechanism of proton-coupled electron transfer regulation.

Main Methods:

  • Fourier Transform Infrared (FT-IR) spectroscopy was used to detect reaction-induced spectral changes.
  • Isotopic labeling with (2)H(4) tyrosine and (15)N tyrosine aided in spectral assignments.
  • Difference spectra were acquired during the reduction of Y122* by hydroxyurea.

Main Results:

  • FT-IR analysis identified specific vibrational bands linked to Y122 (1514 cm(-1)) and Y122* (1498 cm(-1)).
  • Reaction-induced spectra showed changes in amide I bands (1661 and 1652 cm(-1)), indicating structural alterations.
  • These amide band shifts mirrored those observed in a model pentapeptide, suggesting sequence-mediated effects.

Conclusions:

  • The reduction of Y122* is coupled to structural perturbations of nearby amide bonds.
  • These structural changes are influenced by the amino acid sequence surrounding the tyrosyl radical.
  • A proposed mechanism involves redox-linked electrostatic changes within the tyrosyl radical's aromatic ring driving amide bond perturbations.