Conservation of triplet-triplet energy transfer photoprotective pathways in fucoxanthin chlorophyll-binding proteins across algal lineages

Biochim Biophys Acta Bioenerg. 2023 Apr 1;1864(2):148935. doi: 10.1016/j.bbabio.2022.148935. Epub 2022 Nov 13.

Abstract

Detailed information on the photo-generated triplet states of diatom and haptophyte Fucoxanthin Chlorophyll-binding Proteins (FCPs and E-FCPs, respectively) have been obtained from a combined spectroscopic investigation involving Transient Absorption and Time-Resolved Electron Paramagnetic Resonance. Pennate diatom Phaeodactylum tricornutum FCP shows identical photoprotective Triplet-Triplet Energy Transfer (TTET) pathways to the previously investigated centric diatom Cyclotella meneghiniana FCP, with the same two chlorophyll a-fucoxanthin pairs that involve the fucoxanthins in sites Fx301 and Fx302 contributing to TTET in both diatom groups. In the case of the haptophyte Emilianina huxleyi E-FCP, only one of the two chlorophyll a-fucoxanthins pairs observed in diatoms, the one involving chlorophyll a409 and Fx301, has been shown to be active in TTET. Furthermore, despite the marked change in the pigment content of E-FCP with growth light intensity, the TTET pathway is not affected. Thus, our comparative investigation of FCPs revealed a photoprotective TTET pathway shared within these classes involving the fucoxanthin in site Fx301, a site exposed to the exterior of the antenna monomer that has no equivalent in Light-Harvesting Complexes from the green lineage.

Keywords: Carotenoid; Diatom; Emiliania huxleyi; Light-harvesting complex; Photoprotection; TR-EPR.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chlorophyll / metabolism
  • Chlorophyll A / metabolism
  • Chlorophyll Binding Proteins* / chemistry
  • Diatoms* / chemistry
  • Electron Spin Resonance Spectroscopy
  • Energy Transfer

Substances

  • Chlorophyll Binding Proteins
  • Chlorophyll A
  • fucoxanthin
  • Chlorophyll