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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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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

Updated: Jul 12, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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Published on: June 27, 2014

Protein-Solvent Interface Controls Proton-Coupled Reactivity in Cryptochrome 4a.

Jiate Luo1, Matthew Tremblay1, Jonathan Hungerland2

  • 1Department of Chemistry, Princeton University, Princeton, New Jersey 08544, United States.

Journal of the American Chemical Society
|July 10, 2026
PubMed
Summary

This study explores how proton reactions in cryptochrome 4a (Cry4a) affect avian navigation. It reveals that proton-coupled electron transfer pathways can compete with radical pair recombination, influencing magnetic sensitivity.

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Published on: June 15, 2017

Area of Science:

  • Biophysics
  • Quantum Biology
  • Avian Navigation

Background:

  • Cryptochrome 4a (Cry4a) is a proposed radical pair magnetoreceptor for avian navigation.
  • Electron transfer in Cry4a generates radical pairs influencing magnetic sensitivity.
  • Proton-related reactions modulating these spin dynamics are poorly understood.

Purpose of the Study:

  • Investigate deprotonation of tryptophan radical cations in Cry4a.
  • Explore potential proton-coupled electron transfer (PCET) pathways involving tyrosine.
  • Understand how proton transfer affects Cry4a's magnetic sensitivity.

Main Methods:

  • Classical molecular dynamics simulations.
  • Quantum mechanical/molecular mechanical (QM/MM) free energy simulations.
  • Analysis of tryptophan deprotonation and PCET pathways.

Main Results:

  • Limited solvent accessibility suppresses deprotonation of the third tryptophan.
  • The fourth tryptophan is more readily deprotonated.
  • A PCET pathway involving tyrosine and interfacial water shows sub-microsecond kinetics.

Conclusions:

  • Proton transfer and PCET reactions at the protein-solvent interface compete with radical pair recombination.
  • These competing pathways can influence magnetic sensitivity in Cry4a.
  • Establishes a framework for studying proton-coupled processes in cryptochrome-based magnetoreception.