Photosystem I light-harvesting complex Lhca4 adopts multiple conformations: red forms and excited-state quenching are mutually exclusive

Autor: Emilie Wientjes, Francesca Passarini, Roberta Croce, Herbert van Amerongen

Publikováno v: Biochimica et Biophysica Acta (BBA)-Bioenergetics, 11, 1289-1296. Elsevier
Biochimica et Biophysica Acta, 1797(4), 501-508
Biochimica et Biophysica Acta. B, Bioenergetics, 1797(4), 501-508
Biochimica et Biophysica Acta. B, Bioenergetics 1797 (2010) 4
Passarini, F, Wientjes, I E, van Amerongen, H & Croce, R 2010, ' Photosystem I light-harvesting complex Lhca4 adopts multiple conformations: red forms and excited-state quenching are mutually exclusive ', Biochimica et Biophysica Acta (BBA)-Bioenergetics, vol. 11, pp. 1289-1296 . https://doi.org/10.1016/j.bbabio.2010.01.015

In this work we have investigated the origin of the multi-exponential fluorescence decay and of the short excited-state lifetime of Lhca4. Lhca4 is the antenna complex of Photosystem I which accommodates the red-most chlorophyll forms and it has been

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c430690f4b0f3df62a74e329fc996203
https://doi.org/10.1016/j.bbabio.2010.01.015

Towards in vivo mutation analysis: Knock-out of specific chlorophylls bound to the light-harvesting complexes of Arabidopsis thaliana - The case of CP24 (Lhcb6)

Autor: Jacques Hille, Francesca Passarini, Pengqi Xu, Stefano Caffarri, Roberta Croce

Publikováno v: Passarini, F, Xu, P, Caffarri, S, Hille, J & Croce, R 2014, ' Towards in vivo mutation analysis: Knock-out of specific chlorophylls bound to the light-harvesting complexes of Arabidopsis thaliana-The case of CP24 (Lhcb6) ', Biochimica et Biophysica Acta (BBA)-Bioenergetics, vol. 1837, no. 9, pp. 1500-1506 . https://doi.org/10.1016/j.bbabio.2014.02.012
Biochimica biophysica acta (BBA)-Bioenergetics
Biochimica biophysica acta (BBA)-Bioenergetics, Elsevier, 2014, 1837 (9), pp.1500-1506. ⟨10.1016/j.bbabio.2014.02.012⟩
Biochimica biophysica acta (BBA)-Bioenergetics, 2014, 1837 (9), pp.1500-1506. ⟨10.1016/j.bbabio.2014.02.012⟩
Biochimica et Biophysica Acta-Bioenergetics, 1837(9), 1500-1506
Biochimica et Biophysica Acta (BBA)-Bioenergetics, 1837(9), 1500-1506. Elsevier

In the last ten years, a large series of studies have targeted antenna complexes of plants (Lhc) with the aim of understanding the mechanisms of light harvesting and photoprotection. Combining spectroscopy, modeling and mutation analyses, the role of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7a6e31b8b25efc7b834c0209b1dfaf8
https://hdl.handle.net/1871.1/87f70777-6683-4c18-a428-0b6a840c7ea3

Functional analysis of Photosystem I light-harvesting complexes (Lhca) gene products of Chlamydomonas reinhardtii

Autor: Stefano Caffarri, Manuela Mantelli, Roberta Croce, Roberto Bassi, Francesca Passarini, Milena Mozzo

Publikováno v: Biochimica et Biophysica Acta, 1797(2), 212-221
Biochimica biophysica acta (BBA)-Bioenergetics
Biochimica biophysica acta (BBA)-Bioenergetics, Elsevier, 2010, 1797 (2), pp.212-221. ⟨10.1016/j.bbabio.2009.10.005⟩
Biochimica biophysica acta (BBA)-Bioenergetics, 2010, 1797 (2), pp.212-221. ⟨10.1016/j.bbabio.2009.10.005⟩
Biochimica et Biophysica Acta (BBA)-Bioenergetics, 1797, 212-221. Elsevier
Mozzo, M, Mantelli, M, Passarini, F, Caffarri, S, Croce, R & Bassi, R 2010, ' Functional analysis of phoyosystem I light-harvesting complexes (Lhca) gene products of Chlamydomonas reinhardtii ', Biochimica et Biophysica Acta (BBA)-Bioenergetics, vol. 1797, pp. 212-221 . https://doi.org/10.1016/j.bbabio.2009.10.005

The outer antenna system of Chlamydomonas reinhardtii Photosystem I is composed of nine gene products, but due to difficulty in purification their individual properties are not known. In this work, the functional properties of the nine Lhca antennas

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc45a03abe85884a9b207ef16791812b
https://research.rug.nl/en/publications/07f968f2-0d60-4697-8a78-94a1cff077b1

A specific binding site for neoxanthin in the monomeric antenna proteins CP26 and CP29 of Photosystem II

Autor: Roberta Croce, Stefano Caffarri, Roberto Bassi, Francesca Passarini

Publikováno v: FEBS letters
581 (2007): 4704–4710.
info:cnr-pdr/source/autori:Caffarri S., Passarini F., Bassi R. and Croce R./titolo:A specific binding site for neoxanthin in the monomeric antenna proteins CP26 and CP29 of Photosystem II/doi:/rivista:FEBS letters (Print)/anno:2007/pagina_da:4704/pagina_a:4710/intervallo_pagine:4704–4710/volume:581
FEBS Letters, 581(24), 4704-4710. Elsevier
Caffarri, S, Passarini, F, Bassi, R & Croce, R 2007, ' A specific binding site for neoxanthin in the monomeric antenna proteins CP26 and CP29 of Photosystem II ', FEBS Letters, vol. 581, no. 24, pp. 4704-4710 . https://doi.org/10.1016/j.febslet.2007.08.066
FEBS Letters, 581(24), 4704-4710. Wiley

The location of the neoxanthin binding site in CP26 and CP29 was investigated by site-directed mutagenesis. The crystallographic structure of LHCII shows that the binding of neoxanthin to the NI site is stabilised by an H bond with a tyrosine in the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fca52361c294f8b7171cec1be667d9e
http://www.cnr.it/prodotto/i/9641

Identifying the Quencher of Excited State Energy in Photosynthetic Antennae

Autor: Herbert van Amerongen, Patricia M. Dijkman, Rob B. M. Koehorst, Roberta Croce, Milena Mozzo, Francesca Passarini

Publikováno v: CIÊNCIAVITAE
Biophysical Journal, 98(3), 171A-172A. CELL PRESS
ResearcherID

Excess energy dissipation in plants in high-light conditions requires the formation of a quenching site. Although several different quenching mechanisms have been proposed, all of them involve pigment-pigment interactions between chromophores coordin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc082dfefaf756d9fc39690edb622d66
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000208762001356&KeyUID=WOS:000208762001356