Unexpected electron transfer in cryptochrome identified by time-resolved EPR spectroscopy

Angew Chem Int Ed Engl. 2011 Dec 23;50(52):12647-51. doi: 10.1002/anie.201104321. Epub 2011 Nov 15.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cryptochromes / chemistry*
  • Electron Spin Resonance Spectroscopy
  • Electron Transport
  • Photochemical Processes
  • Synechocystis / chemistry
  • Time Factors
  • Xenopus laevis

Substances

  • Cryptochromes