Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Monitoring interfacial bioelectrochemistry using a FRET switch.

J J Davis1, H Burgess, G Zauner

  • 1Central Research Laboratory, Mansfield Road, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QR, United Kingdom.

The Journal of Physical Chemistry. B
|October 13, 2006
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Sierpiński carpet-inspired hierarchical patterning of porous materials for sound absorption.

NPJ acoustics·2025
Same author

Evaluation of re-depositing hydropower trapped sediments at large rivers to improve flood protection and aquatic habitats - Case study Danube/Austria.

The Science of the total environment·2023
Same author

Direct visualization and correlation of liver stereotactic body radiation therapy treatment delivery accuracy with interfractional motion.

Journal of applied clinical medical physics·2021
Same author

Predicting Antimicrobial Resistance Using Partial Genome Alignments.

mSystems·2021
Same author

Evaluation of undetected cases during the COVID-19 epidemic in Austria.

BMC infectious diseases·2021
Same author

The effect of fluorescent labeling on α-synuclein fibril morphology.

Biochimica et biophysica acta·2016
Same journal

From Cation Solvation to Anion Coordination: Lewis-Acidic Boranes Enable Halide Salt Electrolytes.

The journal of physical chemistry. B·2026
Same journal

In Vitro-Prepared A30P Alpha-Synuclein Fibrils Adopt the Conserved and Disease-Relevant Greek Key Fold.

The journal of physical chemistry. B·2026
Same journal

Metastructure Analysis of Self-Assembled Nanocubes with Different Equatorial Methyl Groups Based on Molecular Dynamics Simulations.

The journal of physical chemistry. B·2026
Same journal

A Cocoordinated <sup>1</sup>H Internal Reference Quantifies Proton-Exchange Bias in Coordinated-Water Diffusion.

The journal of physical chemistry. B·2026
Same journal

Unveiling Electrolyte-Dependent Coordination Site Dynamics for Redox Mediator Design in Lithium-O<sub>2</sub> Batteries: Exchange vs Rearrangement.

The journal of physical chemistry. B·2026
Same journal

The Role of Functional Groups in Substituted Benzoic Acids Used as Dopants in Liquid Crystal Mixtures on the Nematic-Isotropic Transitions.

The journal of physical chemistry. B·2026
See all related articles

Researchers developed a new optical method to monitor protein redox states. This technique uses a dye attached to azurin protein, enabling sensitive detection down to zeptomolar levels for biophysical analyses.

Area of Science:

  • Biophysical Chemistry
  • Analytical Chemistry
  • Protein Science

Background:

  • Monitoring the redox state of immobilized proteins is crucial for analytical and biophysical studies.
  • Current methods face limitations due to slow electron-transfer kinetics and poor signal-to-noise ratios.

Purpose of the Study:

  • To develop a sensitive optical method for monitoring the redox state of proteins.
  • To overcome limitations of existing techniques for analyzing protein redox activity at the molecular level.

Main Methods:

  • Covalently tethering a dye to the copper protein azurin.
  • Establishing a highly oxidation-state-sensitive Förster Resonance Energy Transfer (FRET) process.
  • Optically monitoring redox switching at the zeptomolar protein concentration limit.

Related Experiment Videos

Main Results:

  • Demonstrated optical monitoring of redox switching in azurin down to the zeptomolar level.
  • Achieved a highly oxidation-state-sensitive FRET process using a dye-tethered protein.
  • Enabled determination of redox potential for small clusters of molecules via surface-potential-induced emission cycling.

Conclusions:

  • The developed FRET-based method offers unprecedented sensitivity for monitoring protein redox states.
  • This technique advances analytical science and biophysical analyses by enabling molecular-level insights.
  • The method allows for the determination of redox potential from limited numbers of molecules.