Jump to main content
Jump to site search

Issue 32, 2012
Previous Article Next Article

The road not taken: a theoretical view of an unexpected cryptochrome charge transfer path

Author affiliations

Abstract

Motivated by recent progress in electron paramagnetic resonance spectroscopy, we describe hole transfer along a chain of tryptophan amino acids within the cryptochrome protein of Synechocystis sp.: surprisingly, despite a close sequential and structural similarity to E. coli DNA photolyase, the charge transfer paths and the final sites of charge localization are different for these two enzymes. We study this phenomenon using atomistic simulations and electronic structure computations as a theoretical basis, and we take a new look at the concepts of charge transfer and introduce a modification of Marcus' theory that incorporates dynamic polarization effects. Only this variant of theory describes the population of the correct branch on the subnanosecond time scale. Based on our numerical analysis, we further suggest that the Asp372–Arg374 salt bridge acts as a novel stepping stone in the charge transfer reaction.

Graphical abstract: The road not taken: a theoretical view of an unexpected cryptochrome charge transfer path

Back to tab navigation

Publication details

The article was received on 13 Mar 2012, accepted on 27 Jun 2012 and first published on 27 Jun 2012


Article type: Paper
DOI: 10.1039/C2CP40793K
Citation: Phys. Chem. Chem. Phys., 2012,14, 11518-11524
  •   Request permissions

    The road not taken: a theoretical view of an unexpected cryptochrome charge transfer path

    S. Krapf, S. Weber and T. Koslowski, Phys. Chem. Chem. Phys., 2012, 14, 11518
    DOI: 10.1039/C2CP40793K

Search articles by author

Spotlight

Advertisements