A Förster-resonance-energy transfer-based method for fluorescence detection of the protein redox state

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...

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Veröffentlicht in:	Analytical biochemistry 2006-03, Vol.350 (1), p.52-60
Hauptverfasser:	Kuznetsova, Sofya, Zauner, Gerhild, Schmauder, Ralf, Mayboroda, Oleg A., Deelder, André M., Aartsma, Thijs J., Canters, Gerard W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Azurin Azurin - chemistry Carbocyanines - chemistry Copper - chemistry Cytochrome Cytochrome c Group - chemistry Flavodoxin Flavodoxin - chemistry Fluorescence Resonance Energy Transfer - methods Fluorescent Dyes - chemistry Midpoint potential Oxidation-Reduction Potentiometry Proteins - chemistry Redox state Resonance energy transfer Spectrometry, Fluorescence Spectrometry, Mass, Electrospray Ionization - methods
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Beschreibung
Zusammenfassung:	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.
ISSN:	0003-2697 1096-0309
DOI:	10.1016/j.ab.2005.11.036