Excited state dynamics of a PYP chromophore model system explored with ultrafast infrared spectroscopy

Anwar Usman; Omar F. Mohammed; Karsten Heyne; Jens Dreyer; Erik T.J. Nibbering

doi:10.1016/j.cplett.2004.11.032

Excited state dynamics of a PYP chromophore model system explored with ultrafast infrared spectroscopy

Anwar Usman, Omar F. Mohammed, Karsten Heyne, Jens Dreyer, Erik T.J. Nibbering

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

27 Scopus citations

Abstract

We perform ultrafast polarization sensitive visible pump-infrared probe spectroscopy on deprotonated trans-S-phenyl-thio-p-hydroxycinnamate, a model compound for photoactive yellow protein. We derive structural information from the observed bleach signals by comparison of the experimental frequency positions and anisotropies with results from quantum chemical calculations. The electronically excited state decays with 8 or 15 ps time constants for 1:1 or 10:1 DMSO:buffer, respectively, with a quantum yield for isomerization product formation less than 5%. Comparison of our results with earlier reported work on model compounds and on photoactive yellow protein (PYP) suggests an intricate tuning mechanism of the protein environment for the relaxation dynamics of PYP.

Original language	English (US)
Pages (from-to)	157-163
Number of pages	7
Journal	Chemical Physics Letters
Volume	401
Issue number	1-3
DOIs	https://doi.org/10.1016/j.cplett.2004.11.032
State	Published - Jan 1 2005
Externally published	Yes

ASJC Scopus subject areas

General Physics and Astronomy
Physical and Theoretical Chemistry

Access to Document

10.1016/j.cplett.2004.11.032

Cite this

@article{87a453e9538d4119970e7f906d45a15c,

title = "Excited state dynamics of a PYP chromophore model system explored with ultrafast infrared spectroscopy",

abstract = "We perform ultrafast polarization sensitive visible pump-infrared probe spectroscopy on deprotonated trans-S-phenyl-thio-p-hydroxycinnamate, a model compound for photoactive yellow protein. We derive structural information from the observed bleach signals by comparison of the experimental frequency positions and anisotropies with results from quantum chemical calculations. The electronically excited state decays with 8 or 15 ps time constants for 1:1 or 10:1 DMSO:buffer, respectively, with a quantum yield for isomerization product formation less than 5%. Comparison of our results with earlier reported work on model compounds and on photoactive yellow protein (PYP) suggests an intricate tuning mechanism of the protein environment for the relaxation dynamics of PYP.",

author = "Anwar Usman and Mohammed, {Omar F.} and Karsten Heyne and Jens Dreyer and Nibbering, {Erik T.J.}",

year = "2005",

month = jan,

day = "1",

doi = "10.1016/j.cplett.2004.11.032",

language = "English (US)",

volume = "401",

pages = "157--163",

journal = "Chemical Physics Letters",

issn = "0009-2614",

publisher = "Elsevier B.V.",

number = "1-3",

}

TY - JOUR

T1 - Excited state dynamics of a PYP chromophore model system explored with ultrafast infrared spectroscopy

AU - Usman, Anwar

AU - Mohammed, Omar F.

AU - Heyne, Karsten

AU - Dreyer, Jens

AU - Nibbering, Erik T.J.

PY - 2005/1/1

Y1 - 2005/1/1

N2 - We perform ultrafast polarization sensitive visible pump-infrared probe spectroscopy on deprotonated trans-S-phenyl-thio-p-hydroxycinnamate, a model compound for photoactive yellow protein. We derive structural information from the observed bleach signals by comparison of the experimental frequency positions and anisotropies with results from quantum chemical calculations. The electronically excited state decays with 8 or 15 ps time constants for 1:1 or 10:1 DMSO:buffer, respectively, with a quantum yield for isomerization product formation less than 5%. Comparison of our results with earlier reported work on model compounds and on photoactive yellow protein (PYP) suggests an intricate tuning mechanism of the protein environment for the relaxation dynamics of PYP.

AB - We perform ultrafast polarization sensitive visible pump-infrared probe spectroscopy on deprotonated trans-S-phenyl-thio-p-hydroxycinnamate, a model compound for photoactive yellow protein. We derive structural information from the observed bleach signals by comparison of the experimental frequency positions and anisotropies with results from quantum chemical calculations. The electronically excited state decays with 8 or 15 ps time constants for 1:1 or 10:1 DMSO:buffer, respectively, with a quantum yield for isomerization product formation less than 5%. Comparison of our results with earlier reported work on model compounds and on photoactive yellow protein (PYP) suggests an intricate tuning mechanism of the protein environment for the relaxation dynamics of PYP.

UR - http://www.scopus.com/inward/record.url?scp=10644256714&partnerID=8YFLogxK

U2 - 10.1016/j.cplett.2004.11.032

DO - 10.1016/j.cplett.2004.11.032

M3 - Article

AN - SCOPUS:10644256714

SN - 0009-2614

VL - 401

SP - 157

EP - 163

JO - Chemical Physics Letters

JF - Chemical Physics Letters

IS - 1-3

ER -

Excited state dynamics of a PYP chromophore model system explored with ultrafast infrared spectroscopy

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this