title: Unexpected electron transfer in cryptochrome identified by time-resolved EPR spectroscopy.
abstract: 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.
authors.affiliation: Fachberich Physik, Freie Universität Berlin, Germany.
authors.forename: Till
authors.initials: T
authors.lastname: Biskup
authors.forename: Kenichi
authors.initials: K
authors.lastname: Hitomi
authors.forename: Elizabeth D
authors.initials: ED
authors.lastname: Getzoff
authors.forename: Sebastian
authors.initials: S
authors.lastname: Krapf
authors.forename: Thorsten
authors.initials: T
authors.lastname: Koslowski
authors.forename: Erik
authors.initials: E
authors.lastname: Schleicher
authors.forename: Stefan
authors.initials: S
authors.lastname: Weber
mesh_terms: D000818:Animals; D056931:Cryptochromes / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D055668:Photochemical Processes; D046939:Synechocystis / Q000737:chemistry; D013997:Time Factors; D014982:Xenopus laevis
chemical_list: D056931:Cryptochromes
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