Unfolding of the C-Terminal Jα Helix in the LOV2 Photoreceptor Domain Observed by Time-Resolved Vibrational Spectroscopy

P.E. Konold; T. Mathes; J. Weissenborn; M.L. Groot; P. Hegemann; J.T.M. Kennis

doi:10.1021/acs.jpclett.6b01484

Unfolding of the C-Terminal Jα Helix in the LOV2 Photoreceptor Domain Observed by Time-Resolved Vibrational Spectroscopy

P.E. Konold, T. Mathes, J. Weissenborn, M.L. Groot, P. Hegemann, J.T.M. Kennis^*

^*Corresponding author for this work

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Light-triggered reactions of biological photoreceptors have gained immense attention for their role as molecular switches in their native organisms and for optogenetic application. The light, oxygen, and voltage 2 (LOV2) sensing domain of plant phototropin binds a C-terminal Jα helix that is docked on a β-sheet and unfolds upon light absorption by the flavin mononucleotide (FMN) chromophore. In this work, the signal transduction pathway of LOV2 from Avena sativa was investigated using time-resolved infrared spectroscopy from picoseconds to microseconds. In D

Original language	English
Pages (from-to)	3472-3476
Journal	Journal of Physical Chemistry Letters
Volume	7
Issue number	17
DOIs	https://doi.org/10.1021/acs.jpclett.6b01484
Publication status	Published - 2016

Access to Document

10.1021/acs.jpclett.6b01484

Persistent URL (handle)

Copy link address

Cite this

@article{4cf782c904734185b19a4cd4abb66790,

title = "Unfolding of the C-Terminal Jα Helix in the LOV2 Photoreceptor Domain Observed by Time-Resolved Vibrational Spectroscopy",

abstract = "Light-triggered reactions of biological photoreceptors have gained immense attention for their role as molecular switches in their native organisms and for optogenetic application. The light, oxygen, and voltage 2 (LOV2) sensing domain of plant phototropin binds a C-terminal Jα helix that is docked on a β-sheet and unfolds upon light absorption by the flavin mononucleotide (FMN) chromophore. In this work, the signal transduction pathway of LOV2 from Avena sativa was investigated using time-resolved infrared spectroscopy from picoseconds to microseconds. In D",

author = "P.E. Konold and T. Mathes and J. Weissenborn and M.L. Groot and P. Hegemann and J.T.M. Kennis",

year = "2016",

doi = "10.1021/acs.jpclett.6b01484",

language = "English",

volume = "7",

pages = "3472--3476",

journal = "Journal of Physical Chemistry Letters",

issn = "1948-7185",

publisher = "American Chemical Society",

number = "17",

}

TY - JOUR

T1 - Unfolding of the C-Terminal Jα Helix in the LOV2 Photoreceptor Domain Observed by Time-Resolved Vibrational Spectroscopy

AU - Konold, P.E.

AU - Mathes, T.

AU - Weissenborn, J.

AU - Groot, M.L.

AU - Hegemann, P.

AU - Kennis, J.T.M.

PY - 2016

Y1 - 2016

N2 - Light-triggered reactions of biological photoreceptors have gained immense attention for their role as molecular switches in their native organisms and for optogenetic application. The light, oxygen, and voltage 2 (LOV2) sensing domain of plant phototropin binds a C-terminal Jα helix that is docked on a β-sheet and unfolds upon light absorption by the flavin mononucleotide (FMN) chromophore. In this work, the signal transduction pathway of LOV2 from Avena sativa was investigated using time-resolved infrared spectroscopy from picoseconds to microseconds. In D

AB - Light-triggered reactions of biological photoreceptors have gained immense attention for their role as molecular switches in their native organisms and for optogenetic application. The light, oxygen, and voltage 2 (LOV2) sensing domain of plant phototropin binds a C-terminal Jα helix that is docked on a β-sheet and unfolds upon light absorption by the flavin mononucleotide (FMN) chromophore. In this work, the signal transduction pathway of LOV2 from Avena sativa was investigated using time-resolved infrared spectroscopy from picoseconds to microseconds. In D

U2 - 10.1021/acs.jpclett.6b01484

DO - 10.1021/acs.jpclett.6b01484

M3 - Article

SN - 1948-7185

VL - 7

SP - 3472

EP - 3476

JO - Journal of Physical Chemistry Letters

JF - Journal of Physical Chemistry Letters

IS - 17

ER -

Unfolding of the C-Terminal Jα Helix in the LOV2 Photoreceptor Domain Observed by Time-Resolved Vibrational Spectroscopy

Abstract

Access to Document

Persistent URL (handle)

Fingerprint

Cite this