Excitation relaxation dynamics and energy transfer in fucoxanthin- chlorophyll a/c-protein complexes, probed by time-resolved fluorescence
Open accessAbstract
In algae, light-harvesting complexes contain specific chlorophylls (Chls) and keto-carotenoids; Chl a, Chl c, and fucoxanthin (Fx) in diatoms and brown algae; Chl a, Chl c, and peridinin in photosynthetic dinoflagellates; and Chl a, Chl b, and siphonaxanthin in green algae. The Fx-Chl a/c-protein (FCP) complex from the diatom Chaetoceros gracilis contains Chl c1, Chl c2, and the keto-carotenoid, Fx, as antenna pigments, in addition to Chl a. In the present study, we investigated energy transfer in the FCP complex associated with photosystem II (FCPII) of C. gracilis. For these investigations, we analyzed time-resolved fluorescence spectra, fluorescence rise and decay curves, and time-resolved fluorescence anisotropy data. Chl a exhibited different energy forms with fluorescence peaks ranging from 677 nm to 688 nm. Fx transferred excitation energy to lower-energy Chl a with a time constant of 300fs. Chl c transferred excitation energy to Chl a with time constants of 500-600fs (intra-complex transfer), 600-700fs (intra-complex transfer), and 4-6ps (inter-complex transfer). The latter process made a greater contribution to total Chl c-to-Chl a transfer in intact cells of C. gracilis than in the isolated FCPII complexes. The lower-energy Chl a received excitation energy from Fx and transferred the energy to higher-energy Chl a. This article is part of a special issue entitled: photosynthesis research for sustainability: keys to produce clean energy.
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All fluorescence spectra demonstrate an emission band with a maximum at about 686 nm, which corresponds to chlorophyll a, and a broad shoulder at 715-740 nm.
“All spectra demonstrate an emission band with a maximum at about 686 nm, which corresponds to chlorophyll a [[11], [12], [13], [14], [15],39,40], and a broad shoulder at 715–740 nm [39,40].”
From Photoacoustic and fluorescence lifetime imaging of diatoms (2020) · cites this paper as [13]
Section 3.1 reports a chlorophyll a fluorescence peak at 677 nm and a vibrational band around 735 nm in the FCPII spectrum. This supports the attribution of the main emission to chlorophyll a and a longer-wavelength feature, but not a maximum at about 686 nm or the assertion that all spectra show both features. Section 3.3 also describes time-dependent changes in the spectra. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe band at about 628 nm was assigned to chlorophyll c.
“The band at about 628 nm was assigned to chlorophyll c [[11], [12], [13], [14], [15],41,42].”
From Photoacoustic and fluorescence lifetime imaging of diatoms (2020) · cites this paper as [13]
Section 3.1 assigns a nearby red-region absorption peak to chlorophyll c, but locates it around 634 nm, not about 628 nm. Our copy does not identify a 628-nm band. (LLM, conf=0.83)
Experimental — accuracy not yet measuredThe predominant form of chlorophyll observed in diatoms is chlorophyll a, which absorbs energy in the violet-blue and orange-red regions.
“The predominant form of chlorophyll observed in diatoms is chlorophyll a, which absorbs energy in the violet-blue and orange-red regions [[12], [13], [14], [15]].”
From Photoacoustic and fluorescence lifetime imaging of diatoms (2020) · cites this paper as [13]
The Introduction (page unavailable) says diatom light-harvesting complexes contain chlorophyll a and c, and that chlorophyll a has strong violet and red absorption bands. The Results section on steady-state spectra (page unavailable) reports chlorophyll a absorption peaks at 442 and 672 nm. The paper does not establish that chlorophyll a is the predominant chlorophyll in diatoms. (LLM, conf=0.84)
Experimental — accuracy not yet measuredThe absorbance spectra of more concentrated suspensions of diatoms embedded in agarose gel reveal peaks at about 436 nm and 674 nm, attributable to chlorophyll a.
“The absorbance spectra of more concentrated suspensions of diatoms embedded in agarose gel reveal peaks at about 436 nm and 674 nm, attributable to chlorophyll a (Fig. 4) [[11], [12], [13], [14], [15],[41], [42], [43]].”
From Photoacoustic and fluorescence lifetime imaging of diatoms (2020) · cites this paper as [13]
Section 3.1 assigns absorption peaks at 442 nm and 672 nm to chlorophyll a in an isolated FCPII complex, supporting the identification of nearby peaks as chlorophyll a. It does not report peaks at 436 nm and 674 nm in concentrated diatom suspensions embedded in agarose gel. (LLM, conf=0.84)
Experimental — accuracy not yet measuredThe main carotenoid identified in diatoms is fucoxanthin, which absorbs light in the blue-to-green region of the spectrum.
“The main carotenoid identified in diatoms is fucoxanthin, which absorbs light in the blue-to-green region of the spectrum [11,[13], [14], [15]].”
From Photoacoustic and fluorescence lifetime imaging of diatoms (2020) · cites this paper as [13]
The introductory passages (page unavailable) identify fucoxanthin in diatom light-harvesting complexes and describe it as an antenna pigment harvesting blue-to-green light. They call it one of the main carotenoids in algal light-harvesting complexes, but do not establish that it is the main carotenoid in diatoms overall. (LLM, conf=0.82)
Experimental — accuracy not yet measured
The presence of the carotenoid fucoxanthin is represented by a shoulder at about 500 nm.
“The presence of the carotenoid fucoxanthin is represented by a shoulder at about 500 nm [[11], [12], [13], [14], [15],41,42].”
From Photoacoustic and fluorescence lifetime imaging of diatoms (2020) · cites this paper as [13]
Two types of light-harvesting pigments of diatoms are well documented: chlorophylls and carotenoids.
“Two types of light-harvesting pigments of diatoms are well documented [[11], [12], [13], [14]]: chlorophylls and carotenoids.”
From Photoacoustic and fluorescence lifetime imaging of diatoms (2020) · cites this paper as [13]
Unlike many other types of algae, diatoms also contain chlorophyll c, which absorbs mostly blue and red light.
“Unlike many other types of algae, diatoms also contain chlorophyll c, which absorbs mostly blue and red light [[11], [12], [13]].”
From Photoacoustic and fluorescence lifetime imaging of diatoms (2020) · cites this paper as [13]
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Photoacoustic and fluorescence lifetime imaging of diatoms
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- Authors
- Akimoto, S., Teshigahara, A., Yokono, M., Mimuro, M., Nagao, R., & Tomo, T.
- Affiliations
- Japan Science and Technology Agency (JP)
- Kobe University (JP)
- Kyoto University (JP)
- Nagoya University (JP)
- Tokyo University of Science (JP)
- Corresponding author
- Akimoto, Seiji
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2014-09
- Volume
- 1837
- Issue
- 9
- Pages
- 1514-1521
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2098685234
- Cited by
- 51
- References
- 43
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 7 · 2023: 4 · 2022: 5 · 2021: 3 · 2020: 7 · 2019: 6 · 2018: 4 · 2017: 1 · 2016: 2 · 2015: 7
- FWCI
- 1.37
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Australian Research Council (DP12101360)
- Japan Society for the Promotion of Science (21-2944)
- Precursory Research for Embryonic Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Spectroscopy and Quantum Chemical Studies
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Photochemistry and Electron Transfer Studies
- Keywords
- fucoxanthin, chlorophyll a, chlorophyll c, photosystem II, energy transfer, Chaetoceros gracilis, diatoms, light-harvesting complexes, fluorescence anisotropy, ketocarotenoids
- MeSH terms
- Energy Transfer, Fluorescence Polarization, Spectrometry, Fluorescence, Photosystem II Protein Complex, Chlorophyll Binding Proteins
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