Insights into the structural changes occurring upon photoconversion in the orange carotenoid protein from broadband two-dimensional electronic spectroscopy

Eleonora De Re, Gabriela S. Schlau-Cohen, Ryan L. Leverenz, Vanessa Margaret Huxter, Thomas A A Oliver, Richard A. Mathies, Graham R. Fleming

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Carotenoids play an essential role in photoprotection, interacting with other pigments to safely dissipate excess absorbed energy as heat. In cyanobacteria, the short time scale photoprotective mechanisms involve the photoactive orange carotenoid protein (OCP), which binds a single carbonyl carotenoid. Blue-green light induces the photoswitching of OCP from its ground state form (OCPO) to a metastable photoproduct (OCPR). OCPR can bind to the phycobilisome antenna and induce fluorescence quenching. The photoswitching is accompanied by structural and functional changes at the level of the protein and of the bound carotenoid. Here, we use broadband two-dimensional electronic spectroscopy to study the differences in excited state dynamics of the carotenoid in the two forms of OCP. Our results provide insight into the origin of the pronounced vibrational lineshape and oscillatory dynamics observed in linear absorption and 2D electronic spectroscopy of OCPO and the large inhomogeneous broadening in OCPR, with consequences for the chemical function of the two forms.

Original languageEnglish (US)
Pages (from-to)5382-5389
Number of pages8
JournalJournal of Physical Chemistry B
Volume118
Issue number20
DOIs
StatePublished - May 22 2014
Externally publishedYes

Fingerprint

carotenoids
Carotenoids
Spectrum Analysis
Spectroscopy
broadband
proteins
Proteins
electronics
spectroscopy
Phycobilisomes
Methyl Green
Cyanobacteria
pigments
Excited states
Pigments
Ground state
Quenching
antennas
Hot Temperature
Fluorescence

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Materials Chemistry
  • Surfaces, Coatings and Films
  • Medicine(all)

Cite this

Insights into the structural changes occurring upon photoconversion in the orange carotenoid protein from broadband two-dimensional electronic spectroscopy. / De Re, Eleonora; Schlau-Cohen, Gabriela S.; Leverenz, Ryan L.; Huxter, Vanessa Margaret; Oliver, Thomas A A; Mathies, Richard A.; Fleming, Graham R.

In: Journal of Physical Chemistry B, Vol. 118, No. 20, 22.05.2014, p. 5382-5389.

Research output: Contribution to journalArticle

De Re, Eleonora ; Schlau-Cohen, Gabriela S. ; Leverenz, Ryan L. ; Huxter, Vanessa Margaret ; Oliver, Thomas A A ; Mathies, Richard A. ; Fleming, Graham R. / Insights into the structural changes occurring upon photoconversion in the orange carotenoid protein from broadband two-dimensional electronic spectroscopy. In: Journal of Physical Chemistry B. 2014 ; Vol. 118, No. 20. pp. 5382-5389.
@article{eae0856856d4436e811b4d1bed7a1f0d,
title = "Insights into the structural changes occurring upon photoconversion in the orange carotenoid protein from broadband two-dimensional electronic spectroscopy",
abstract = "Carotenoids play an essential role in photoprotection, interacting with other pigments to safely dissipate excess absorbed energy as heat. In cyanobacteria, the short time scale photoprotective mechanisms involve the photoactive orange carotenoid protein (OCP), which binds a single carbonyl carotenoid. Blue-green light induces the photoswitching of OCP from its ground state form (OCPO) to a metastable photoproduct (OCPR). OCPR can bind to the phycobilisome antenna and induce fluorescence quenching. The photoswitching is accompanied by structural and functional changes at the level of the protein and of the bound carotenoid. Here, we use broadband two-dimensional electronic spectroscopy to study the differences in excited state dynamics of the carotenoid in the two forms of OCP. Our results provide insight into the origin of the pronounced vibrational lineshape and oscillatory dynamics observed in linear absorption and 2D electronic spectroscopy of OCPO and the large inhomogeneous broadening in OCPR, with consequences for the chemical function of the two forms.",
author = "{De Re}, Eleonora and Schlau-Cohen, {Gabriela S.} and Leverenz, {Ryan L.} and Huxter, {Vanessa Margaret} and Oliver, {Thomas A A} and Mathies, {Richard A.} and Fleming, {Graham R.}",
year = "2014",
month = "5",
day = "22",
doi = "10.1021/jp502120h",
language = "English (US)",
volume = "118",
pages = "5382--5389",
journal = "Journal of Physical Chemistry B Materials",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "20",

}

TY - JOUR

T1 - Insights into the structural changes occurring upon photoconversion in the orange carotenoid protein from broadband two-dimensional electronic spectroscopy

AU - De Re, Eleonora

AU - Schlau-Cohen, Gabriela S.

AU - Leverenz, Ryan L.

AU - Huxter, Vanessa Margaret

AU - Oliver, Thomas A A

AU - Mathies, Richard A.

AU - Fleming, Graham R.

PY - 2014/5/22

Y1 - 2014/5/22

N2 - Carotenoids play an essential role in photoprotection, interacting with other pigments to safely dissipate excess absorbed energy as heat. In cyanobacteria, the short time scale photoprotective mechanisms involve the photoactive orange carotenoid protein (OCP), which binds a single carbonyl carotenoid. Blue-green light induces the photoswitching of OCP from its ground state form (OCPO) to a metastable photoproduct (OCPR). OCPR can bind to the phycobilisome antenna and induce fluorescence quenching. The photoswitching is accompanied by structural and functional changes at the level of the protein and of the bound carotenoid. Here, we use broadband two-dimensional electronic spectroscopy to study the differences in excited state dynamics of the carotenoid in the two forms of OCP. Our results provide insight into the origin of the pronounced vibrational lineshape and oscillatory dynamics observed in linear absorption and 2D electronic spectroscopy of OCPO and the large inhomogeneous broadening in OCPR, with consequences for the chemical function of the two forms.

AB - Carotenoids play an essential role in photoprotection, interacting with other pigments to safely dissipate excess absorbed energy as heat. In cyanobacteria, the short time scale photoprotective mechanisms involve the photoactive orange carotenoid protein (OCP), which binds a single carbonyl carotenoid. Blue-green light induces the photoswitching of OCP from its ground state form (OCPO) to a metastable photoproduct (OCPR). OCPR can bind to the phycobilisome antenna and induce fluorescence quenching. The photoswitching is accompanied by structural and functional changes at the level of the protein and of the bound carotenoid. Here, we use broadband two-dimensional electronic spectroscopy to study the differences in excited state dynamics of the carotenoid in the two forms of OCP. Our results provide insight into the origin of the pronounced vibrational lineshape and oscillatory dynamics observed in linear absorption and 2D electronic spectroscopy of OCPO and the large inhomogeneous broadening in OCPR, with consequences for the chemical function of the two forms.

UR - http://www.scopus.com/inward/record.url?scp=84901355724&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84901355724&partnerID=8YFLogxK

U2 - 10.1021/jp502120h

DO - 10.1021/jp502120h

M3 - Article

VL - 118

SP - 5382

EP - 5389

JO - Journal of Physical Chemistry B Materials

JF - Journal of Physical Chemistry B Materials

SN - 1520-6106

IS - 20

ER -