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 the primary light reaction of cryptochrome in animal magnetoreception.
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. pavel.muller@cea.fr klaus.brettel@cea.fr.
Pavel
P
Müller
Junpei
J
Yamamoto
Ryan
R
Martin
Shigenori
S
Iwai
Klaus
K
Brettel
D000818:Animals; D056931:Cryptochromes / Q000737:chemistry / Q000378:metabolism*; D004255:Deoxyribodipyrimidine Photo-Lyase / Q000737:chemistry / Q000378:metabolism*; D004330:Drosophila / Q000201:enzymology / Q000378:metabolism*; D004579:Electron Transport; D008958:Models, Molecular; D014364:Tryptophan / Q000737:chemistry / Q000378:metabolism*
D056931:Cryptochromes; D014364:Tryptophan; D004255:Deoxyribodipyrimidine Photo-Lyase