| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1176729 | Analytical Biochemistry | 2006 | 9 Pages |
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.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Sofya Kuznetsova, Gerhild Zauner, Ralf Schmauder, Oleg A. Mayboroda, André M. Deelder, Thijs J. Aartsma, Gerard W. Canters,