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Fluorescence and Excited-State Confo...
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Gurchiek, Jason.
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Fluorescence and Excited-State Conformational Dynamics of Ketocarotenoids in the Orange Carotenoid Protein.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Fluorescence and Excited-State Conformational Dynamics of Ketocarotenoids in the Orange Carotenoid Protein./
作者:
Gurchiek, Jason.
出版者:
Ann Arbor : ProQuest Dissertations & Theses, : 2021,
面頁冊數:
151 p.
附註:
Source: Dissertations Abstracts International, Volume: 82-11, Section: B.
Contained By:
Dissertations Abstracts International82-11B.
標題:
Physical chemistry. -
電子資源:
https://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=28496663
ISBN:
9798738621833
Fluorescence and Excited-State Conformational Dynamics of Ketocarotenoids in the Orange Carotenoid Protein.
Gurchiek, Jason.
Fluorescence and Excited-State Conformational Dynamics of Ketocarotenoids in the Orange Carotenoid Protein.
- Ann Arbor : ProQuest Dissertations & Theses, 2021 - 151 p.
Source: Dissertations Abstracts International, Volume: 82-11, Section: B.
Thesis (Ph.D.)--Michigan State University, 2021.
This item must not be sold to any third party vendors.
The Orange Carotenoid Protein (OCP) mediates nonphotochemical quenching (NPQ) mechanisms in cyanobacteria using a bound ketocarotenoid as a sensor of light intensity and as a quencher of phycocyanobilin excitons in the phycobilisome. During periods of high light intensity, the protein undergoes a conversion from a resting, orange state (OCPO) to an active, red state (OCPR) after optical preparation of the S2 state of the ketocarotenoid. The mechanism by which this conversion is photochemically initiated remains an open question. We determined that the spectrum, polarization, and quantum yield of fluorescence from two examples of ketocarotenoids bound in OCPO, 3'-hydroxyechinenone and canthaxanthin, reveal important details of the dynamics that follow optical preparation of the S2 state. Additionally, by measuring the fluorescence emission anisotropy of a prototype carotenoid, β-carotene, we observed large-amplitude distortions after the S2 state passes over a low activation-energy barrier that are consistent with twisting and pyramidalization near the center of the isoprenoid backbone. These results indicate that the ketocarotenoid is poised in OCPO in a distorted conformation from which the photoactivation reaction is triggered by further excited-state torsional distortions of the conjugated polyene backbone.
ISBN: 9798738621833Subjects--Topical Terms:
1981412
Physical chemistry.
Subjects--Index Terms:
Carotenoid fluorescence
Fluorescence and Excited-State Conformational Dynamics of Ketocarotenoids in the Orange Carotenoid Protein.
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The Orange Carotenoid Protein (OCP) mediates nonphotochemical quenching (NPQ) mechanisms in cyanobacteria using a bound ketocarotenoid as a sensor of light intensity and as a quencher of phycocyanobilin excitons in the phycobilisome. During periods of high light intensity, the protein undergoes a conversion from a resting, orange state (OCPO) to an active, red state (OCPR) after optical preparation of the S2 state of the ketocarotenoid. The mechanism by which this conversion is photochemically initiated remains an open question. We determined that the spectrum, polarization, and quantum yield of fluorescence from two examples of ketocarotenoids bound in OCPO, 3'-hydroxyechinenone and canthaxanthin, reveal important details of the dynamics that follow optical preparation of the S2 state. Additionally, by measuring the fluorescence emission anisotropy of a prototype carotenoid, β-carotene, we observed large-amplitude distortions after the S2 state passes over a low activation-energy barrier that are consistent with twisting and pyramidalization near the center of the isoprenoid backbone. These results indicate that the ketocarotenoid is poised in OCPO in a distorted conformation from which the photoactivation reaction is triggered by further excited-state torsional distortions of the conjugated polyene backbone.
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