Hydrogen Bond Switching among Flavin and Amino Acid Side Chains in the BLUF Photoreceptor Observed by Ultrafast Infrared Spectroscopy

C. Bonetti, T. Mathes, I.H.M. van Stokkum, K.M. Mullen, R. van Grondelle, M.L. Groot, P. Hegemann, J.T.M. Kennis

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

BLUF domains constitute a recently discovered class of photoreceptor proteins found in bacteria and eukaryotic algae. BLUF domains are blue-light sensitive through a FAD cofactor that is involved in an extensive hydrogen-bond network with nearby amino acid side chains, including a highly conserved tyrosine and glutamine. The participation of particular amino acid side chains in the ultrafast hydrogen-bond switching reaction with FAD that underlies photoactivation of BLUF domains is assessed by means of ultrafast infrared spectroscopy. Blue-light absorption by FAD results in formation of FAD
Original languageEnglish
Pages (from-to)4790-4802
JournalBiophysical Journal
Volume95
Issue number10
DOIs
Publication statusPublished - 2008

Bibliographical note

Hydrogen Bond Switching among Flavin and Amino Acid Side Chains in the BLUF Photoreceptor Observed by Ultrafast Infrared Spectroscopy

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