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New roles of flavoproteins in molecular cell biology: Blue‐light active flavoproteins studied by electron paramagnetic resonance
Author(s) -
Schleicher Erik,
Bittl Robert,
Weber Stefan
Publication year - 2009
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2009.07141.x
Subject(s) - flavoprotein , cryptochrome , electron paramagnetic resonance , electron paramagnetic resonance spectroscopy , protonation , chemistry , flavin group , unpaired electron , spectroscopy , nuclear magnetic resonance spectroscopy , photochemistry , enzyme , nuclear magnetic resonance , biochemistry , stereochemistry , physics , organic chemistry , quantum mechanics , gene , ion , circadian clock
Exploring enzymatic mechanisms at a molecular level is one of the major challenges in modern biophysics. Based on enzyme structure data, as obtained by X‐ray crystallography or NMR spectroscopy, one can suggest how substrates and products bind for catalysis. However, from the 3D structure alone it is very rarely possible to identify how intermediates are formed and how they are interconverted. Molecular spectroscopy can provide such information and thus supplement our knowledge on the specific enzymatic reaction under consideration. In the case of enzymatic processes in which paramagnetic molecules play a role, EPR and related methods such as electron‐nuclear double resonance (ENDOR) are powerful techniques to unravel important details, e.g. the electronic structure or the protonation state of the intermediate(s) carrying (the) unpaired electron spin(s). Here, we review recent EPR/ENDOR studies of blue‐light active flavoproteins with emphasis on photolyases that catalyze the enzymatic repair of UV damaged DNA, and on cryptochrome blue‐light photoreceptors that act in several species as central components of the circadian clock.