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Angew Chem Int Ed Engl
2011 Dec 23;5052:12647-51. doi: 10.1002/anie.201104321.
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Unexpected electron transfer in cryptochrome identified by time-resolved EPR spectroscopy.
Biskup T
,
Hitomi K
,
Getzoff ED
,
Krapf S
,
Koslowski T
,
Schleicher E
,
Weber S
.
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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.
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