Carotenoid-protein interaction alters the S-1 energy of hydroxyechinenone in the Orange Carotenoid Protein
(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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- author
- Polivka, Tomas ; Chabera, Pavel LU and Kerfeld, Cheryl A.
- organization
- publishing date
- 2013
- type
- 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
- additional info
- 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)
- id
- 262c16f5-b954-42a3-99ad-60becc1e15a7 (old id 3671486)
- date added to LUP
- 2016-04-01 13:48:18
- date last changed
- 2023-11-12 22:09:39
@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}},
keywords = {{Photoprotection; Cyanobacteria; Carotenoid; Orange Carotenoid Protein; Femtosecond transient absorption spectroscopy}},
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}},
}