Femtosecond stimulated Raman study of the photoactive flavoprotein AppABLUF

Christopher R. Hall; Ismael A. Heisler; Garth A. Jones; James E. Frost; Agnieszka A. Gil; Peter J. Tonge; Stephen R. Meech

doi:10.1016/j.cplett.2017.03.030

Femtosecond stimulated Raman study of the photoactive flavoprotein AppA_BLUF

Christopher R. Hall
, Ismael A. Heisler
, Garth A. Jones
, James E. Frost
, Agnieszka A. Gil
, Peter J. Tonge
, Stephen R. Meech

Chemistry

University of East Anglia
Stony Brook University

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

Femtosecond stimulated Raman spectroscopy (FSRS) is applied to study the photocycle of a blue light using flavin (BLUF) domain photoreceptor, AppA_BLUF. It is shown that FSRS spectra are sensitive to the light adapted state of the protein and probe its excited state dynamics. The dominant contribution to the most sensitive excited state Raman active modes is from flavin ring modes. However, TD-DFT calculations for excited state structures indicate that reproduction and assignment of the experimentally observed spectral shift will require high level calculations on the flavin in its specific protein environment.

Original language	English
Pages (from-to)	365-369
Number of pages	5
Journal	Chemical Physics Letters
Volume	683
DOIs	https://doi.org/10.1016/j.cplett.2017.03.030
State	Published - Sep 1 2017

Access to Document

10.1016/j.cplett.2017.03.030

Cite this

@article{ae5902c714b44315b750db94ccb8724d,

title = "Femtosecond stimulated Raman study of the photoactive flavoprotein AppABLUF",

abstract = "Femtosecond stimulated Raman spectroscopy (FSRS) is applied to study the photocycle of a blue light using flavin (BLUF) domain photoreceptor, AppABLUF. It is shown that FSRS spectra are sensitive to the light adapted state of the protein and probe its excited state dynamics. The dominant contribution to the most sensitive excited state Raman active modes is from flavin ring modes. However, TD-DFT calculations for excited state structures indicate that reproduction and assignment of the experimentally observed spectral shift will require high level calculations on the flavin in its specific protein environment.",

author = "Hall, \{Christopher R.\} and Heisler, \{Ismael A.\} and Jones, \{Garth A.\} and Frost, \{James E.\} and Gil, \{Agnieszka A.\} and Tonge, \{Peter J.\} and Meech, \{Stephen R.\}",

note = "Publisher Copyright: {\textcopyright} 2017 Elsevier B.V.",

year = "2017",

month = sep,

day = "1",

doi = "10.1016/j.cplett.2017.03.030",

language = "English",

volume = "683",

pages = "365--369",

journal = "Chemical Physics Letters",

issn = "0009-2614",

}

TY - JOUR

T1 - Femtosecond stimulated Raman study of the photoactive flavoprotein AppABLUF

AU - Hall, Christopher R.

AU - Heisler, Ismael A.

AU - Jones, Garth A.

AU - Frost, James E.

AU - Gil, Agnieszka A.

AU - Tonge, Peter J.

AU - Meech, Stephen R.

PY - 2017/9/1

Y1 - 2017/9/1

N2 - Femtosecond stimulated Raman spectroscopy (FSRS) is applied to study the photocycle of a blue light using flavin (BLUF) domain photoreceptor, AppABLUF. It is shown that FSRS spectra are sensitive to the light adapted state of the protein and probe its excited state dynamics. The dominant contribution to the most sensitive excited state Raman active modes is from flavin ring modes. However, TD-DFT calculations for excited state structures indicate that reproduction and assignment of the experimentally observed spectral shift will require high level calculations on the flavin in its specific protein environment.

AB - Femtosecond stimulated Raman spectroscopy (FSRS) is applied to study the photocycle of a blue light using flavin (BLUF) domain photoreceptor, AppABLUF. It is shown that FSRS spectra are sensitive to the light adapted state of the protein and probe its excited state dynamics. The dominant contribution to the most sensitive excited state Raman active modes is from flavin ring modes. However, TD-DFT calculations for excited state structures indicate that reproduction and assignment of the experimentally observed spectral shift will require high level calculations on the flavin in its specific protein environment.

UR - https://www.scopus.com/pages/publications/85015990462

U2 - 10.1016/j.cplett.2017.03.030

DO - 10.1016/j.cplett.2017.03.030

M3 - Article

AN - SCOPUS:85015990462

SN - 0009-2614

VL - 683

SP - 365

EP - 369

JO - Chemical Physics Letters

JF - Chemical Physics Letters

ER -

Femtosecond stimulated Raman study of the photoactive flavoprotein AppA_BLUF

Abstract

Access to Document

Other files and links

Fingerprint

Cite this