photosynthetic NADP+ reduction / photosystem I stabilization / chloroplast photosystem I / response to low light intensity stimulus / chloroplast stromal thylakoid / plastoglobule / chloroplast membrane / response to high light intensity / chloroplast thylakoid / photosynthesis, light harvesting in photosystem I ...photosynthetic NADP+ reduction / photosystem I stabilization / chloroplast photosystem I / response to low light intensity stimulus / chloroplast stromal thylakoid / plastoglobule / chloroplast membrane / response to high light intensity / chloroplast thylakoid / photosynthesis, light harvesting in photosystem I / thylakoid / chloroplast envelope / photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / plastid / chlorophyll binding / chloroplast thylakoid membrane / photosynthesis / response to cold / chloroplast / 4 iron, 4 sulfur cluster binding / electron transfer activity / oxidoreductase activity / protein stabilization / protein domain specific binding / mRNA binding / magnesium ion binding / mitochondrion / extracellular region / metal ion binding / nucleus / cytosol 類似検索 - 分子機能
Photosystem I reaction centre subunit N, chloroplastic / Photosystem I reaction centre subunit N superfamily / Photosystem I reaction centre subunit N (PSAN or PSI-N) / Photosystem I PsaH, reaction centre subunit VI / Photosystem I reaction centre subunit VI / Photosystem I reaction center subunit V / 4Fe-4S dicluster domain / Photosystem I reaction center subunit psaK, plant / Photosystem I reaction center subunit V/PsaK, plant / Photosystem I PsaG/PsaK domain, chloroplastic ...Photosystem I reaction centre subunit N, chloroplastic / Photosystem I reaction centre subunit N superfamily / Photosystem I reaction centre subunit N (PSAN or PSI-N) / Photosystem I PsaH, reaction centre subunit VI / Photosystem I reaction centre subunit VI / Photosystem I reaction center subunit V / 4Fe-4S dicluster domain / Photosystem I reaction center subunit psaK, plant / Photosystem I reaction center subunit V/PsaK, plant / Photosystem I PsaG/PsaK domain, chloroplastic / Photosystem I reaction centre subunit PsaK superfamily / Photosystem I psaG and psaK proteins signature. / Photosystem I reaction center subunit V/PsaK / Photosystem I psaG / psaK / Photosystem I PsaL, reaction centre subunit XI / Photosystem I, reaction centre subunit XI / Photosystem I PsaL, reaction centre subunit XI superfamily / Photosystem I reaction centre subunit XI / Photosystem I reaction centre subunit VIII / Photosystem I reaction centre subunit VIII / Photosystem I reaction centre subunit VIII superfamily / Photosystem I PsaF, reaction centre subunit III / Photosystem I PsaF, reaction centre subunit III superfamily / Photosystem I reaction centre subunit III / Photosystem I PsaD / Photosystem I, reaction centre subunit PsaD superfamily / PsaD / Photosystem I PsaE, reaction centre subunit IV / Photosystem I reaction centre subunit IV / PsaE / Photosystem I PsaJ, reaction centre subunit IX superfamily / Photosystem I PsaJ, reaction centre subunit IX / Photosystem I reaction centre subunit IX / PsaJ / Chlorophyll A-B binding protein, plant and chromista / Chlorophyll A-B binding protein / Chlorophyll A-B binding protein / Photosystem I protein PsaC / Photosystem I PsaA / Photosystem I PsaB / Photosystem I PsaA/PsaB, conserved site / Photosystem I psaA and psaB proteins signature. / : / Photosystem I PsaA/PsaB / Photosystem I PsaA/PsaB superfamily / Photosystem I psaA/psaB protein / Electron transport accessory-like domain superfamily / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain 類似検索 - ドメイン・相同性
Photosystem I reaction center subunit IX / Photosystem I P700 chlorophyll a apoprotein A2 / Photosystem I P700 chlorophyll a apoprotein A1 / Chlorophyll a-b binding protein 4, chloroplastic / Photosystem I reaction center subunit N, chloroplastic / Photosystem I reaction center subunit VIII / Photosystem I iron-sulfur center / Chlorophyll a-b binding protein 6, chloroplastic / Photosystem I reaction center subunit IV B, chloroplastic / Photosystem I reaction center subunit V, chloroplastic ...Photosystem I reaction center subunit IX / Photosystem I P700 chlorophyll a apoprotein A2 / Photosystem I P700 chlorophyll a apoprotein A1 / Chlorophyll a-b binding protein 4, chloroplastic / Photosystem I reaction center subunit N, chloroplastic / Photosystem I reaction center subunit VIII / Photosystem I iron-sulfur center / Chlorophyll a-b binding protein 6, chloroplastic / Photosystem I reaction center subunit IV B, chloroplastic / Photosystem I reaction center subunit V, chloroplastic / Photosystem I reaction center subunit II-2, chloroplastic / Photosystem I reaction center subunit III, chloroplastic / Photosystem I reaction center subunit XI, chloroplastic / Photosystem I reaction center subunit psaK, chloroplastic / Photosystem I reaction center subunit VI-1, chloroplastic / Photosystem I chlorophyll a/b-binding protein 3-1, chloroplastic / Photosystem I chlorophyll a/b-binding protein 2, chloroplastic 類似検索 - 構成要素
ジャーナル: New Phytol / 年: 2025 タイトル: Structural determinants for red-shifted absorption in higher-plants Photosystem I. 著者: Stefano Capaldi / Zeno Guardini / Daniele Montepietra / Vittorio Flavio Pagliuca / Antonello Amelii / Elena Betti / Chris John / Laura Pedraza-González / Lorenzo Cupellini / Benedetta ...著者: Stefano Capaldi / Zeno Guardini / Daniele Montepietra / Vittorio Flavio Pagliuca / Antonello Amelii / Elena Betti / Chris John / Laura Pedraza-González / Lorenzo Cupellini / Benedetta Mennucci / Diane Marie Valerie Bonnet / Antonio Chaves-Sanjuan / Luca Dall'Osto / Roberto Bassi / 要旨: Higher plants Photosystem I absorbs far-red light, enriched under vegetation canopies, through long-wavelength Chls to enhance photon capture. Far-red absorption originates from Chl pairs within the ...Higher plants Photosystem I absorbs far-red light, enriched under vegetation canopies, through long-wavelength Chls to enhance photon capture. Far-red absorption originates from Chl pairs within the Lhca3 and Lhca4 subunits of the LHCI antenna, known as the 'red cluster', including Chls a603 and a609. We used reverse genetics to produce an Arabidopsis mutant devoid of red-shifted absorption, and we obtained high-resolution cryogenic electron microscopy structures of PSI-LHCI complexes from both wild-type and mutant plants. Computed excitonic coupling values suggested contributions from additional nearby pigment molecules, namely Chl a615 and violaxanthin in the L2 site, to far-red absorption. We investigated the structural determinants of far-red absorption by producing further Arabidopsis transgenic lines and analyzed the spectroscopic effects of mutations targeting these chromophores. The two structures solved were used for quantum mechanics calculations, revealing that excitonic interactions alone cannot explain far-red absorption, while charge transfer states were needed for accurate spectral simulations. Our findings demonstrate that the molecular mechanisms of light-harvesting under shaded conditions rely on very precise tuning of chromophore interactions, whose understanding is crucial for designing light-harvesting complexes with engineered absorption spectra.