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

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...

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Veröffentlicht in:	Chemical communications (Cambridge, England) England), 2015-01, Vol.51 (85), p.15502-15505
Hauptverfasser:	Müller, Pavel, Yamamoto, Junpei, Martin, Ryan, Iwai, Shigenori, Brettel, Klaus
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Cryptochromes - chemistry Cryptochromes - metabolism Deoxyribodipyrimidine Photo-Lyase - chemistry Deoxyribodipyrimidine Photo-Lyase - metabolism Drosophila - enzymology Drosophila - metabolism Electron Transport Functional analysis Life Sciences Models, Molecular Radicals Tryptophan Tryptophan - chemistry Tryptophan - metabolism
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Beschreibung
Zusammenfassung:	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.
ISSN:	1359-7345 1364-548X
DOI:	10.1039/c5cc06276d