Evidence for reversible light-dependent transitions in the photosynthetic pigments of diatoms. Issue 49 (3rd November 2022)
- Record Type:
- Journal Article
- Title:
- Evidence for reversible light-dependent transitions in the photosynthetic pigments of diatoms. Issue 49 (3rd November 2022)
- Main Title:
- Evidence for reversible light-dependent transitions in the photosynthetic pigments of diatoms
- Authors:
- Tselios, Charalampos
Varotsis, Constantinos - Abstract:
- Abstract : A reversible light-intensity behavior of Dds and Fxs composition in the cells of T. pseudonana . The observed LL to HL reversible transitions are accompanied by structural modifications of Chls a / c and the lack of the red-shifted Fxs. Abstract : Marine diatoms contribute to oxygenic photosynthesis and carbon fixation and handle large changes under variable light intensity on a regular basis. The unique light-harvesting apparatus of diatoms are the fucoxanthin–chlorophyll a / c -binding proteins (FCPs). Here, we show the enhancement of chlorophyll a / c (Chl a / c ), fucoxanthin (Fx), and diadinoxanthin (Dd) marker bands in the Raman spectra of the centric diatom T. pseudonana, which allows distinction of the pigment content in the cells grown under low- (LL) and high-light (HL) intensity at room temperature. Reversible LL–HL dependent conformations of Chl c, characteristic of two conformations of the porphyrin macrocycle, and the presence of five- and six-coordinated Chl a / c with weak axial ligands are observed in the Raman data. Under HL the energy transfer from Chl c to Chl a is reduced and that from the red-shifted Fxs is minimal. Therefore, Chl c and the blue-shifted Fxs are the only contributors to the energy transfer pathways under HL and the blue- to red-shifted Fxs energy transfer pathway characteristic of the LL is inactive. The results indicate that T. pseudonana can redirect its function from light harvesting to energy-quenching state, andAbstract : A reversible light-intensity behavior of Dds and Fxs composition in the cells of T. pseudonana . The observed LL to HL reversible transitions are accompanied by structural modifications of Chls a / c and the lack of the red-shifted Fxs. Abstract : Marine diatoms contribute to oxygenic photosynthesis and carbon fixation and handle large changes under variable light intensity on a regular basis. The unique light-harvesting apparatus of diatoms are the fucoxanthin–chlorophyll a / c -binding proteins (FCPs). Here, we show the enhancement of chlorophyll a / c (Chl a / c ), fucoxanthin (Fx), and diadinoxanthin (Dd) marker bands in the Raman spectra of the centric diatom T. pseudonana, which allows distinction of the pigment content in the cells grown under low- (LL) and high-light (HL) intensity at room temperature. Reversible LL–HL dependent conformations of Chl c, characteristic of two conformations of the porphyrin macrocycle, and the presence of five- and six-coordinated Chl a / c with weak axial ligands are observed in the Raman data. Under HL the energy transfer from Chl c to Chl a is reduced and that from the red-shifted Fxs is minimal. Therefore, Chl c and the blue-shifted Fxs are the only contributors to the energy transfer pathways under HL and the blue- to red-shifted Fxs energy transfer pathway characteristic of the LL is inactive. The results indicate that T. pseudonana can redirect its function from light harvesting to energy-quenching state, and reversibly to light-harvesting upon subsequent illumination to LL by reproducing the red-shifted Fxs and decrease the number of Dds. The LL to HL reversible transitions are accompanied by structural modifications of Chl a / c and the lack of the red-shifted Fxs. … (more)
- Is Part Of:
- RSC advances. Volume 12:Issue 49(2022)
- Journal:
- RSC advances
- Issue:
- Volume 12:Issue 49(2022)
- Issue Display:
- Volume 12, Issue 49 (2022)
- Year:
- 2022
- Volume:
- 12
- Issue:
- 49
- Issue Sort Value:
- 2022-0012-0049-0000
- Page Start:
- 31555
- Page End:
- 31563
- Publication Date:
- 2022-11-03
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d2ra05284a ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 24360.xml