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Carotenoid-protein interaction alters the S-1 energy of hydroxyechinenone in the Orange Carotenoid Protein

Polivka, Tomas ; Chabera, Pavel LU and Kerfeld, Cheryl A. (2013) In Biochimica et Biophysica Acta - Bioenergetics 1827(3). p.248-254
Abstract
The Orange Carotenoid Protein (OCP) is a photoactive water soluble protein that is crucial for photoprotection in cyanobacteria. When activated by blue-green light, it triggers quenching of phycobilisome fluorescence and regulates energy flow from the phycobilisome to the reaction center. The OCP contains a single pigment, the carotenoid 3'-hydroxyechinenone (hECN). Binding to the OCP causes a conformational change in hECN leading to an extension of its effective conjugation length. We have determined the S-1 energy of hECN in organic solvent and compared it with the S-1 energy of hECN bound to the OCP. In methanol and n-hexane, hECN has an S-1 energy of 14,300 cm(-1), slightly higher than carotenoids with shorter conjugation lengths such... (More)
The Orange Carotenoid Protein (OCP) is a photoactive water soluble protein that is crucial for photoprotection in cyanobacteria. When activated by blue-green light, it triggers quenching of phycobilisome fluorescence and regulates energy flow from the phycobilisome to the reaction center. The OCP contains a single pigment, the carotenoid 3'-hydroxyechinenone (hECN). Binding to the OCP causes a conformational change in hECN leading to an extension of its effective conjugation length. We have determined the S-1 energy of hECN in organic solvent and compared it with the S-1 energy of hECN bound to the OCP. In methanol and n-hexane, hECN has an S-1 energy of 14,300 cm(-1), slightly higher than carotenoids with shorter conjugation lengths such as zeaxanthin or beta-carotene; this is consistent with the proposal that the presence of the conjugated carbonyl group in hECN increases its Si energy. The S-1 energy of hECN in organic solvent is independent of solvent polarity. Upon binding to the OCP, the S-1 energy of hECN is further increased to 14,700 cm(-1), underscoring the importance of protein binding which twists the conjugated carbonyl group into s-trans conformation and enhances the effect of the carbonyl group. Activated OCP, however, has an S-1 energy of 14,000 cm(-1), indicating that significant changes in the vicinity of the conjugated carbonyl group occur upon activation. (C) 2012 Elsevier B.V. All rights reserved. (Less)
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Contribution to journal
publication status
published
subject
keywords
Photoprotection, Cyanobacteria, Carotenoid, Orange Carotenoid Protein, Femtosecond transient absorption spectroscopy
in
Biochimica et Biophysica Acta - Bioenergetics
volume
1827
issue
3
pages
248 - 254
publisher
Elsevier
external identifiers
  • wos:000315249000003
  • scopus:84871987624
  • pmid:23084967
ISSN
0005-2728
DOI
10.1016/j.bbabio.2012.10.005
language
English
LU publication?
yes
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The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Chemical Physics (S) (011001060)
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262c16f5-b954-42a3-99ad-60becc1e15a7 (old id 3671486)
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2016-04-01 13:48:18
date last changed
2020-12-29 04:00:23
@article{262c16f5-b954-42a3-99ad-60becc1e15a7,
  abstract     = {The Orange Carotenoid Protein (OCP) is a photoactive water soluble protein that is crucial for photoprotection in cyanobacteria. When activated by blue-green light, it triggers quenching of phycobilisome fluorescence and regulates energy flow from the phycobilisome to the reaction center. The OCP contains a single pigment, the carotenoid 3'-hydroxyechinenone (hECN). Binding to the OCP causes a conformational change in hECN leading to an extension of its effective conjugation length. We have determined the S-1 energy of hECN in organic solvent and compared it with the S-1 energy of hECN bound to the OCP. In methanol and n-hexane, hECN has an S-1 energy of 14,300 cm(-1), slightly higher than carotenoids with shorter conjugation lengths such as zeaxanthin or beta-carotene; this is consistent with the proposal that the presence of the conjugated carbonyl group in hECN increases its Si energy. The S-1 energy of hECN in organic solvent is independent of solvent polarity. Upon binding to the OCP, the S-1 energy of hECN is further increased to 14,700 cm(-1), underscoring the importance of protein binding which twists the conjugated carbonyl group into s-trans conformation and enhances the effect of the carbonyl group. Activated OCP, however, has an S-1 energy of 14,000 cm(-1), indicating that significant changes in the vicinity of the conjugated carbonyl group occur upon activation. (C) 2012 Elsevier B.V. All rights reserved.},
  author       = {Polivka, Tomas and Chabera, Pavel and Kerfeld, Cheryl A.},
  issn         = {0005-2728},
  language     = {eng},
  number       = {3},
  pages        = {248--254},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta - Bioenergetics},
  title        = {Carotenoid-protein interaction alters the S-1 energy of hydroxyechinenone in the Orange Carotenoid Protein},
  url          = {http://dx.doi.org/10.1016/j.bbabio.2012.10.005},
  doi          = {10.1016/j.bbabio.2012.10.005},
  volume       = {1827},
  year         = {2013},
}