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Photosynthetic growth despite a broken Q-cycle
Institut de Biologie Physico-Chimique, Paris, France.ORCID iD: 0000-0002-8777-3174
2011 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 2, no 1, article id 301Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
Macmillan Publishers Ltd., 2011. Vol. 2, no 1, article id 301
Keywords [en]
Benzoquinones, Chlamydomonas reinhardtii/*enzymology/genetics/growth & development, Cytochrome b6f Complex/analysis/genetics/*metabolism, Cytochromes f/metabolism, Electron Transport, Heme/deficiency, Hydroquinones, Immunoblotting, Mutation, Oxidoreductases/*metabolism, Photosynthesis/*physiology
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:umu:diva-144809DOI: 10.1038/ncomms1299ISI: 000294802600006PubMedID: 21556055Scopus ID: 2-s2.0-79955919132OAI: oai:DiVA.org:umu-144809DiVA, id: diva2:1182878
Available from: 2018-02-14 Created: 2018-02-14 Last updated: 2023-03-28Bibliographically approved

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Publisher's full textPubMedScopushttp://www.ncbi.nlm.nih.gov/pubmed/21556055

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CiteExportLink to record
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