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

doi:10.1529/biophysj.108.139246

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 Journal › Article › Academic › peer-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 language	English
Pages (from-to)	4790-4802
Journal	Biophysical Journal
Volume	95
Issue number	10
DOIs	https://doi.org/10.1529/biophysj.108.139246
Publication status	Published - 2008

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

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10.1529/biophysj.108.139246

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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",

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T1 - Hydrogen Bond Switching among Flavin and Amino Acid Side Chains in the BLUF Photoreceptor Observed by Ultrafast Infrared Spectroscopy

AU - Bonetti, C.

AU - Mathes, T.

AU - van Stokkum, I.H.M.

AU - Mullen, K.M.

AU - van Grondelle, R.

AU - Groot, M.L.

AU - Hegemann, P.

AU - Kennis, J.T.M.

N1 - Hydrogen Bond Switching among Flavin and Amino Acid Side Chains in the BLUF Photoreceptor Observed by Ultrafast Infrared Spectroscopy

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AB - 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

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DO - 10.1529/biophysj.108.139246

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VL - 95

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JO - Biophysical Journal

JF - Biophysical Journal

IS - 10

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

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