Issue 85, 2015
From the journal:

Chemical Communications

Discovery and functional analysis of a 4th electron-transferring tryptophan conserved exclusively in animal cryptochromes and (6-4) photolyases†

Pavel Müller,*a   Junpei Yamamoto,b   Ryan Martin,c   Shigenori Iwaib  and  Klaus Brettel*a  

* Corresponding authors

a Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, CEA Saclay, iBiTec-S/SB2SM, Bât. 532, 91191 Gif-sur-Yvette, France
E-mail: pavel.muller@cea.fr, klaus.brettel@cea.fr

b Division of Chemistry, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan

c Department of Chemistry, UMR 8640 CNRS-ENS-UPMC, Ecole Normale Supérieure, 24 rue Lhomond, 75005 Paris, France

Abstract

A 4th electron transferring tryptophan in animal cryptochromes and (6-4) photolyases is discovered and functionally analyzed by transient absorption. It yields a much longer-lived flavin-tryptophan radical pair than the mere tryptophan triad in related flavoproteins, questioning the putative role of the primary light reaction of cryptochrome in animal magnetoreception.

Graphical abstract: Discovery and functional analysis of a 4th electron-transferring tryptophan conserved exclusively in animal cryptochromes and (6-4) photolyases

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Article information

DOI
https://doi.org/10.1039/C5CC06276D
Article type
Communication
Submitted
27 Jul 2015
Accepted
26 Aug 2015
First published
27 Aug 2015

Chem. Commun., 2015,51, 15502-15505

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Discovery and functional analysis of a 4th electron-transferring tryptophan conserved exclusively in animal cryptochromes and (6-4) photolyases

P. Müller, J. Yamamoto, R. Martin, S. Iwai and K. Brettel, Chem. Commun., 2015, 51, 15502 DOI: 10.1039/C5CC06276D

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