Energy dissipation mechanisms in the FCPb light-harvesting complex of the diatom Cyclotella meneghiniana

Huzifa M.A.M. Elnour, Lars Dietzel, Charusheela Ramanan, Claudia Büchel, Rienk van Grondelle, Tjaart P.J. Krüger

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Transient absorption spectroscopy has been applied to investigate the energy dissipation mechanisms in the nonameric fucoxanthin-chlorophyll-a,c-binding protein FCPb of the centric diatom Cyclotella meneghiniana. FCPb complexes in their unquenched state were compared with those in two types of quenching environments, namely aggregation-induced quenching by detergent removal, and clustering via incorporation into liposomes. Applying global and target analysis, in combination with a fluorescence lifetime study and annihilation calculations, we were able to resolve two quenching channels in FCPb that involve chlorophyll-a pigments for FCPb exposed to both quenching environments. The fast quenching channel operates on a timescale of tens of picoseconds and exhibits similar spectral signatures as the unquenched state. The slower quenching channel operates on a timescale of tens to hundreds of picoseconds, depending on the degree of quenching, and is characterized by enhanced population of low-energy states between 680 and 710 nm. The results indicate that FCPb is, in principle, able to function as a dissipater of excess energy and can do this in vitro even more efficiently than the homologous FCPa complex, the sole complex involved in fast photoprotection in these organisms. This indicates that when a complex displays photoprotection-related spectral signatures in vitro it does not imply that the complex participates in photoprotection in vivo. We suggest that FCPa is favored over FCPb as the sole energy-regulating complex in diatoms because its composition can more easily establish the balance between light-harvesting and quenching required for efficient photoprotection.

Original languageEnglish
Pages (from-to)1151-1160
Number of pages10
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1859
Issue number10
Early online date27 Jul 2018
DOIs
Publication statusPublished - Oct 2018

Fingerprint

Diatoms
Quenching
Energy dissipation
Chlorophyll Binding Proteins
Light
Liposomes
Detergents
Cluster Analysis
Spectrum Analysis
Fluorescence
Population
In Vitro Techniques
Absorption spectroscopy
Pigments
Electron energy levels
Agglomeration
Display devices
chlorophyll a

Keywords

  • Diatom
  • Fucoxanthin-chlorophyll protein
  • Light harvesting antenna
  • Nonphotochemical quenching
  • Proteoliposome
  • Transient absorption spectroscopy

Cite this

Elnour, Huzifa M.A.M. ; Dietzel, Lars ; Ramanan, Charusheela ; Büchel, Claudia ; van Grondelle, Rienk ; Krüger, Tjaart P.J. / Energy dissipation mechanisms in the FCPb light-harvesting complex of the diatom Cyclotella meneghiniana. In: Biochimica et Biophysica Acta - Bioenergetics. 2018 ; Vol. 1859, No. 10. pp. 1151-1160.
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Energy dissipation mechanisms in the FCPb light-harvesting complex of the diatom Cyclotella meneghiniana. / Elnour, Huzifa M.A.M.; Dietzel, Lars; Ramanan, Charusheela; Büchel, Claudia; van Grondelle, Rienk; Krüger, Tjaart P.J.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1859, No. 10, 10.2018, p. 1151-1160.

Research output: Contribution to JournalArticleAcademicpeer-review

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T1 - Energy dissipation mechanisms in the FCPb light-harvesting complex of the diatom Cyclotella meneghiniana

AU - Elnour, Huzifa M.A.M.

AU - Dietzel, Lars

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AU - Büchel, Claudia

AU - van Grondelle, Rienk

AU - Krüger, Tjaart P.J.

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AB - Transient absorption spectroscopy has been applied to investigate the energy dissipation mechanisms in the nonameric fucoxanthin-chlorophyll-a,c-binding protein FCPb of the centric diatom Cyclotella meneghiniana. FCPb complexes in their unquenched state were compared with those in two types of quenching environments, namely aggregation-induced quenching by detergent removal, and clustering via incorporation into liposomes. Applying global and target analysis, in combination with a fluorescence lifetime study and annihilation calculations, we were able to resolve two quenching channels in FCPb that involve chlorophyll-a pigments for FCPb exposed to both quenching environments. The fast quenching channel operates on a timescale of tens of picoseconds and exhibits similar spectral signatures as the unquenched state. The slower quenching channel operates on a timescale of tens to hundreds of picoseconds, depending on the degree of quenching, and is characterized by enhanced population of low-energy states between 680 and 710 nm. The results indicate that FCPb is, in principle, able to function as a dissipater of excess energy and can do this in vitro even more efficiently than the homologous FCPa complex, the sole complex involved in fast photoprotection in these organisms. This indicates that when a complex displays photoprotection-related spectral signatures in vitro it does not imply that the complex participates in photoprotection in vivo. We suggest that FCPa is favored over FCPb as the sole energy-regulating complex in diatoms because its composition can more easily establish the balance between light-harvesting and quenching required for efficient photoprotection.

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