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Updated: Aug 13, 2026

Luminescence Resonance Energy Transfer to Study Conformational Changes in Membrane Proteins Expressed in Mammalian Cells
Published on: September 16, 2014
A Förster-resonance-energy transfer-based method for fluorescence detection of the protein redox state
Sofya Kuznetsova1, Gerhild Zauner, Ralf Schmauder
1Leiden Institute of Chemistry-Gorlaeus Laboratories, Leiden University, The Netherlands.
Abstract:
A method for fluorescence detection of a protein's redox state based on resonance energy transfer from an attached fluorescence label to the prosthetic group of the redox protein is described and tested for proteins containing three types of prosthetic groups: a type-1 copper site (azurin, amicyanin, plastocyanin, and pseudoazurin), a heme group (cytochrome c550), and a flavin mononucleotide (flavodoxin). This method permits one to reliably distinguish between reduced and oxidized proteins and to perform potentiometric titrations at submicromolar concentrations.

