Long-wavelength absorbing antenna pigments and heterogeneous absorption bands concentrate excitons and increase absorption cross section

Trissl, H.‐W.

doi:10.1007/bf00016556

Cited by 146 publications

(110 citation statements)

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“…Red forms in PSI have been suggested to increase light absorption, providing an advantage in a spectrally filtered light caused by self-absorption and shading (51)(52)(53). Alternatively, red forms of PSI have been proposed to play a relevant role in PSI photoprotection by concentrating excitation energy in protein domains specialized for Chl singlet/triplet quenching (54,55).…”

Section: Discussionmentioning

confidence: 99%

A Red-shifted Antenna Protein Associated with Photosystem II in Physcomitrella patens

Alboresi

Gerotto

Cazzaniga

et al. 2011

Journal of Biological Chemistry

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Antenna systems of plants and green algae are made up of pigment-protein complexes belonging to the light-harvesting complex (LHC) multigene family. LHCs increase the light-harvesting cross-section of photosystems I and II and catalyze photoprotective reactions that prevent light-induced damage in an oxygenic environment. The genome of the moss Physcomitrella patens contains two genes encoding LHCb9, a new antenna protein that bears an overall sequence similarity to photosystem II antenna proteins but carries a specific motif typical of photosystem I antenna proteins. This consists of the presence of an asparagine residue as a ligand for Chl 603 (A5) chromophore rather than a histidine, the common ligand in all other LHCbs. Asparagine as a Chl 603 (A5) ligand generates red-shifted spectral forms associated with photosystem I rather than with photosystem II, suggesting that in P. patens, the energy landscape of photosystem II might be different with respect to that of most green algae and plants. In this work, we show that the in vitro refolded LHCb9-pigment complexes carry a red-shifted fluorescence emission peak, different from all other known photosystem II antenna proteins. By using a specific antibody, we localized LHCb9 within PSII supercomplexes in the thylakoid membranes. This is the first report of red-shifted spectral forms in a PSII antenna system, suggesting that this biophysical feature might have a special role either in optimization of light use efficiency or in photoprotection in the specific environmental conditions experienced by this moss.Light energy powers photosynthesis. Sunlight is absorbed by chlorophyll (Chl) 2 and carotenoid molecules bound to protein supercomplexes embedded in thylakoid membranes, called photosystem I and II (PSI and PSII). Each photosystem has two moieties: (i) the core complex and (ii) the peripheral antenna system. The core complex contains mostly plastid-encoded subunits, which are responsible for charge separation and for the first steps of electron transport and are also active in light harvesting. An additional antenna system, made of nucleusencoded subunits binding Chl a, Chl b, and xanthophylls, is localized peripherally in photosystems and is responsible for most light harvesting, transfer of excitation energy to the reaction centers, and photoprotective reactions like ROS scavenging and quenching of triplet and singlet excited states (1-3). Reaction center protein sequences are widely conserved among organisms, and only small differences are found in sequences of oxygenic organism as far apart as higher plants and cyanobacteria (4, 5). Antenna systems are instead more variable, and in land plants and green algae, they are composed of multiple copies of light-harvesting complex (LHC) proteins (4) assembled around core complexes (6). Clustering analysis of LHC protein sequences clearly distinguishes members associated with PSI (LHCa or LHCI) from those belonging to PSII (LHCb or LHCII) (7). In Arabidopsis thaliana, six different polypeptides were identified for...

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Section: Discussionmentioning

confidence: 99%

A Red-shifted Antenna Protein Associated with Photosystem II in Physcomitrella patens

Alboresi

Gerotto

Cazzaniga

et al. 2011

Journal of Biological Chemistry

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“…The cyanobacterium, Acaryochloris marina, which uses Chl d at ~715-720 nm instead of Chl a, may be adapted to receive this remaining longer wavelength filtered through (Scheer, 2003;Trissl, 1993). B. viridis inhabits murky, anoxic sediments where little visible light penetrates.…”

Section: Range Of Photosynthetic Organisms Habitats Pigments Metabmentioning

confidence: 99%

“…anoxygenic photosynthesis occurs at wavelengths as long as 1015-1020 nm (Trissl, 1993;Scheer, et al, 2003).…”

Section: Range Of Photosynthetic Organisms Habitats Pigments Metabmentioning

confidence: 99%

Spectral Signatures of Photosynthesis. I. Review of Earth Organisms

et al. 2007

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Why do plants reflect in the green and have a "red edge" in the red, and should extrasolar photosynthesis be the same? We provide: 1) a brief review of how photosynthesis works; 2) an overview of the diversity of photosynthetic organisms, their light harvesting systems, and environmental ranges; 3) a synthesis of photosynthetic surface spectral signatures; 4) evolutionary rationales for photosynthetic surface reflectance spectra with regard to utilization of photon energy and the planetary light environment. We found the "NIR end" of the red edge to trend from blue-shifted to reddest for (in order): snow algae, temperature algae, lichens, mosses, aquatic plants, and finally terrestrial vascular plants. The red edge is weak or sloping in lichens.Purple bacteria exhibit possibly a sloping edge in the NIR. More studies are needed on pigmentprotein complexes, membrane composition, and measurements of bacteria before firm conclusions can be drawn about the role of the NIR reflectance. Pigment absorbance features are strongly correlated with features of atmospheric spectral transmittance: P680 in PS II with the peak surface incident photon flux density at ~685 nm, just before an oxygen band at 687.5 nm; the NIR end of the red edge with water absorbance bands and the oxygen A-band at 761 nm; and bacteriochlorophyll reaction center wavelengths with local maxima in atmospheric and water transmittance spectra. Given the surface incident photon flux density spectrum and resonance transfer in light harvesting, we propose some rules with regard to where photosynthetic pigments will peak in absorbance: a) the wavelength of peak incident photon flux; b) the longest available wavelength for core antenna or reaction center pigments; and c) the shortest wavelengths within an atmospheric window for accessory pigments. That plants absorb less green light may not be an inefficient legacy of evolutionary history, but may actually satisfy the above criteria.

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“…Long wavelength absorbing chlorophylls (Chls) have been proposed to focus excitation energy to the reaction centre of PS I (Shubin et al 1995), to be an intermediate energy trap (Woolfe et al 1994), to facilitate light absorption (Trissl 1993) and to serve a photoprotective purpose for PS I . The trimerisation of PS I in vivo has been suggested to mediate state transitions in cyanobacteria (Kruip et al 1994).…”

Section: Introductionmentioning

confidence: 99%

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Mangels

Kruip

Berry

et al. 2002

Photosynthesis Research

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Photosystem I from the unusual cyanobacterium Gloeobacter violaceus Mangels, D.; Kruip, J.; Berry, S.; Rögner, M.; Boekema, E.J.; Koenig, F. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Key words: antenna system, electron microscopy, fluorescence, light harvesting, photosynthesis, plasma membrane AbstractPhotosystem I (PS I) from the primitive cyanobacterium Gloeobacter violaceus has been purified and characterised. Despite the fact that the isolated complexes have the same subunit composition as complexes from other cyanobacteria, the amplitude of flash-induced absorption difference spectra indicates a much bigger antenna size with about 150 chlorophylls per P700 as opposed to the usual 90. Image analysis of the PS I preparation from Gloeobacter reveals that the PS I particles exist both in a trimeric and in a monomeric form and that their size and shape closely resembles other cyanobacterial PS I particles. However, the complexes exhibit a higher molecular weight as could be shown by gel filtration. The preparation contains novel polypeptides not related to known Photosystem I subunits. The N-terminal sequence of one of those polypeptides has been determined and reveals no homology to known or hypothetical proteins. Immunoblotting shows a cross-reaction of three of the polypeptide bands with an antibody raised against the major LHC from the diatom Cyclotella cryptica. Electron microscopy reveals a novel T-shaped complex which has never been observed in any other cyanobacterial PS I preparation. 77 K spectra of purified PS I show an extreme blue-shift of the fluorescence emission, indicating an unusual organisation of the PS I antenna system in Gloeobacter.Abbreviations: PS -photosystem; Chl -chlorophyll; DM -dodecyl-β-D-maltoside; ECL -enhanced chemiluminescence; HPLC -high performance liquid chromatography; IEC -ion exchange chromatography; GF -gel filtration; LHC I -light harvesting complex associated with Photosystem I; P700 -primary electron donor of photosystem I; SDS -sodium dodecyl sulfate; SQDG -sulfoquinovosyl diacylglycerol; PAGE -polyacrylamide gel electrophoresis; F760 (F730) -fluorescence band with maximal emission at 760 nm (730 nm)

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Long-wavelength absorbing antenna pigments and heterogeneous absorption bands concentrate excitons and increase absorption cross section

Cited by 146 publications

References 99 publications

A Red-shifted Antenna Protein Associated with Photosystem II in Physcomitrella patens

A Red-shifted Antenna Protein Associated with Photosystem II in Physcomitrella patens

Spectral Signatures of Photosynthesis. I. Review of Earth Organisms

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