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Unexpected Electron Transfer in Cryptochrome Identified by Time‐Resolved EPR Spectroscopy
Author(s) -
Biskup Till,
Hitomi Kenichi,
Getzoff Elizabeth D.,
Krapf Sebastian,
Koslowski Thorsten,
Schleicher Erik,
Weber Stefan
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201104321
Subject(s) - electron paramagnetic resonance , electron transfer , diversity (politics) , cryptochrome , electron , spectroscopy , chemistry , charge (physics) , crystallography , computer science , physics , political science , biochemistry , photochemistry , nuclear magnetic resonance , gene , quantum mechanics , law , circadian clock
Subtle differences in the local sequence and conformation of amino acids can result in diversity and specificity in electron transfer (ET) in proteins, despite structural conservation of the redox partners. For individual ET steps, distance is not necessarily the decisive parameter; orientation and solvent accessibility of the ET partners, and thus the stabilization of the charge‐separated states, contribute substantially.