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Photosynthetic growth despite a broken Q-cycle

Central in respiration or photosynthesis, the cytochrome bc(1) and b(6)f complexes are regarded as functionally similar quinol oxidoreductases. They both catalyse a redox loop, the Q-cycle, which couples electron and proton transfer. This loop involves a bifurcated electron transfer step considered...

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Autores principales: Malnoë, Alizée, Wollman, Francis-André, de Vitry, Catherine, Rappaport, Fabrice
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3112540/
https://www.ncbi.nlm.nih.gov/pubmed/21556055
http://dx.doi.org/10.1038/ncomms1299
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author Malnoë, Alizée
Wollman, Francis-André
de Vitry, Catherine
Rappaport, Fabrice
author_facet Malnoë, Alizée
Wollman, Francis-André
de Vitry, Catherine
Rappaport, Fabrice
author_sort Malnoë, Alizée
collection PubMed
description Central in respiration or photosynthesis, the cytochrome bc(1) and b(6)f complexes are regarded as functionally similar quinol oxidoreductases. They both catalyse a redox loop, the Q-cycle, which couples electron and proton transfer. This loop involves a bifurcated electron transfer step considered as being mechanistically mandatory, making the Q-cycle indispensable for growth. Attempts to falsify this paradigm in the case of cytochrome bc(1) have failed. The rapid proteolytic degradation of b(6)f complexes bearing mutations aimed at hindering the Q-cycle has precluded so far the experimental assessment of this model in the photosynthetic chain. Here we combine mutations in Chlamydomonas that inactivate the redox loop but preserve high accumulation levels of b(6)f complexes. The oxidoreductase activity of these crippled complexes is sufficient to sustain photosynthetic growth, which demonstrates that the Q-cycle is dispensable for oxygenic photosynthesis.
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spelling pubmed-31125402011-06-29 Photosynthetic growth despite a broken Q-cycle Malnoë, Alizée Wollman, Francis-André de Vitry, Catherine Rappaport, Fabrice Nat Commun Article Central in respiration or photosynthesis, the cytochrome bc(1) and b(6)f complexes are regarded as functionally similar quinol oxidoreductases. They both catalyse a redox loop, the Q-cycle, which couples electron and proton transfer. This loop involves a bifurcated electron transfer step considered as being mechanistically mandatory, making the Q-cycle indispensable for growth. Attempts to falsify this paradigm in the case of cytochrome bc(1) have failed. The rapid proteolytic degradation of b(6)f complexes bearing mutations aimed at hindering the Q-cycle has precluded so far the experimental assessment of this model in the photosynthetic chain. Here we combine mutations in Chlamydomonas that inactivate the redox loop but preserve high accumulation levels of b(6)f complexes. The oxidoreductase activity of these crippled complexes is sufficient to sustain photosynthetic growth, which demonstrates that the Q-cycle is dispensable for oxygenic photosynthesis. Nature Publishing Group 2011-05 2011-05-10 /pmc/articles/PMC3112540/ /pubmed/21556055 http://dx.doi.org/10.1038/ncomms1299 Text en Copyright © 2011, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by-nc-sa/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-Share Alike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/
spellingShingle Article
Malnoë, Alizée
Wollman, Francis-André
de Vitry, Catherine
Rappaport, Fabrice
Photosynthetic growth despite a broken Q-cycle
title Photosynthetic growth despite a broken Q-cycle
title_full Photosynthetic growth despite a broken Q-cycle
title_fullStr Photosynthetic growth despite a broken Q-cycle
title_full_unstemmed Photosynthetic growth despite a broken Q-cycle
title_short Photosynthetic growth despite a broken Q-cycle
title_sort photosynthetic growth despite a broken q-cycle
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3112540/
https://www.ncbi.nlm.nih.gov/pubmed/21556055
http://dx.doi.org/10.1038/ncomms1299
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