How can EPR spectroscopy help to unravel molecular mechanisms of flavin-dependent photoreceptors?

Abstract: Electron paramagnetic resonance (EPR) spectroscopy is a well-established spectroscopic method for the examination of paramagnetic molecules. Proteins can contain paramagnetic moieties in form of stable cofactors, transiently formed intermediates, or spin labels artificially introduced to cysteine sites. The focus of this review is to evaluate potential scopes of application of EPR to the emerging field of optogenetics. The main objective for EPR spectroscopy in this context is to unravel the complex mechanisms of light-active proteins, from their primary photoreaction to downstream signal transduction. An overview of recent results from the family of flavin-containing, blue-light dependent photoreceptors is given. In detail, mechanistic similarities and differences are condensed from the three classes of flavoproteins, the cryptochromes, LOV (Light-oxygen-voltage), and BLUF (blue-light using FAD) domains. Additionally, a concept that includes spin-labeled proteins and examination using modern pulsed EPR is introduced, which allows for a precise mapping of light-induced conformational changes

Location
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch

Classification
Biowissenschaften, Biologie
Keyword
Photorezeptor
Elektronenspinresonanzspektroskopie
Entfernungsmessung
Radikal
Flavoenzym

Event
Veröffentlichung
(where)
Freiburg
(who)
Universität
(when)
2018
Creator

DOI
10.3389/fmolb.2015.00049
URN
urn:nbn:de:bsz:25-freidok-166439
Rights
Kein Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
14.08.2025, 10:58 AM CEST

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Associated

Time of origin

  • 2018

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