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Publications (10 of 11) Show all publications
Malnoë, A. (2018). Photoinhibition or photoprotection of photosynthesis?: update on the (newly termed) sustained quenching component qH. Environmental and Experimental Botany, 154, 123-133
Open this publication in new window or tab >>Photoinhibition or photoprotection of photosynthesis?: update on the (newly termed) sustained quenching component qH
2018 (English)In: Environmental and Experimental Botany, ISSN 0098-8472, E-ISSN 1873-7307, Vol. 154, p. 123-133Article, review/survey (Refereed) Published
Abstract [en]

Non-photochemical quenching (NPQ) of chlorophyll fluorescence is a valuable feature for the study of photosynthetic organisms’ light utilization and dissipation. However, all too often NPQ is simply equated with the harmless dissipation of excess absorbed light energy as heat. This is not always the case as some processes cause NPQ without thermal dissipation. Photoinhibitory quenching, qI, is sustained NPQ that continuously depresses the commonly used fluorescence parameter “quantum yield of photosystem II (PSII)”, or Fv/Fm, and is often viewed as a result of PSII core inactivation due to D1 damage. Inactivated PSII cores might have a photoprotective role but that is not the topic of the present review. Instead, this review focuses on a sustained photoprotective antenna quenching component, which we have termed qH, and summarizes the recently uncovered molecular players of this sustained form of NPQ.

Place, publisher, year, edition, pages
Elsevier, 2018
Keywords
Arabidopsis, Energy dissipation, NPQ, Photoinhibition, Photoprotection
National Category
Botany
Identifiers
urn:nbn:se:umu:diva-150141 (URN)10.1016/j.envexpbot.2018.05.005 (DOI)000443669000013 ()2-s2.0-85048152660 (Scopus ID)
Note

Special issue: SI

Available from: 2018-07-10 Created: 2018-07-10 Last updated: 2018-11-05Bibliographically approved
Malnoë, A., Schultink, A., Shahrasbi, S., Rumeau, D., Havaux, M. & Niyogi, K. K. (2017). The Plastid Lipocalin LCNP is Required for Sustained Photoprotective Energy Dissipation in Arabidopsis. Plant Cell, 30, 196-208
Open this publication in new window or tab >>The Plastid Lipocalin LCNP is Required for Sustained Photoprotective Energy Dissipation in Arabidopsis
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2017 (English)In: Plant Cell, Vol. 30, p. 196-208Article in journal (Refereed) Published
Abstract [en]

Light utilization is finely tuned in photosynthetic organisms to prevent cellular damage. The dissipation of excess absorbed light energy, a process termed NPQ, plays an important role in photoprotection. Little is known about the sustained or slowly reversible form(s) of NPQ and whether they are photoprotective, in part due to the lack of mutants. The Arabidopsis thaliana suppressor of quenching1 (soq1) mutant exhibits enhanced sustained NPQ, which we term qH. To identify molecular players involved in qH, we screened for suppressors of soq1 and isolated mutants affecting either chlorophyllide a oxygenase (CAO) or the chloroplastic lipocalin (CHL), now renamed plastid lipocalin (LCNP). Analysis of the mutants confirmed that qH is localized to the peripheral antenna (LHCII) of photosystem II and demonstrated that LCNP is required for qH, either directly (by forming NPQ sites) or indirectly (by modifying the LHCII membrane environment). qH operates under stress conditions such as cold and high light and is photoprotective, as it reduces lipid peroxidation levels. We propose that, under stress conditions, LCNP protects the thylakoid membrane by enabling sustained NPQ in LHCII, thereby preventing singlet oxygen stress.

National Category
Biological Sciences
Identifiers
urn:nbn:se:umu:diva-144801 (URN)1532-298X (Electronic) 1040-4651 (Linking) (ISBN)
Note

Malnoe, Alizee Schultink, Alex Shahrasbi, Sanya Rumeau, Dominique Havaux, Michel Niyogi, Krishna K eng 2017/12/14 06:00 Plant Cell. 2017 Dec 12. pii: tpc.17.00536. doi: 10.1105/tpc.17.00536.

Available from: 2018-02-17 Created: 2018-02-17 Last updated: 2018-06-09
Wang, F., Qi, Y., Malnoë, A., Choquet, Y., Wollman, F. A. & de Vitry, C. (2016). The High Light Response and Redox Control of Thylakoid FtsH Protease in Chlamydomonas reinhardtii. Mol Plant
Open this publication in new window or tab >>The High Light Response and Redox Control of Thylakoid FtsH Protease in Chlamydomonas reinhardtii
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2016 (English)In: Mol PlantArticle in journal (Refereed) Published
Abstract [en]

In Chlamydomonas reinhardtii, the major protease involved in the maintenance of the photosynthetic machinery in thylakoid membranes - the FtsH protease - forms mostly large hetero-oligomers ( approximately 1 MDa) comprising FtsH1 and FtsH2 subunits, whatever the light intensity for growth. Upon high light exposure, the FtsH subunits display a shorter half-life, which is counterbalanced by an increase in FTSH1/2 mRNA levels, resulting in a modest upregulation of FtsH1/2 proteins. Furthermore, we show that high light increases the protease activity through a hitherto unnoticed redox-controlled reduction of intermolecular disulfide bridges. We isolated a Chlamydomonas FTSH1 promoter deficient mutant, ftsh1-3, due to the insertion of a TOC1 transposon. Accordingly, the high light-induced upregulation of FTSH1 gene expression is largely lost. In this mutant, the abundance of the FtsH1 and 2 proteins are loosely coupled (respectively decreased by 70 and 30%) with no formation of large and stable homo-oligomers. Using strains exhibiting different accumulation levels of the FtsH1 subunit after complementation of the ftsh1-3 mutant, we demonstrate that high light tolerance is tightly correlated with the abundance of the FtsH protease. Thus, the response of Chlamydomonas to light stress involves higher levels of FtsH1/2 subunits associated into large complexes with increased proteolytic activity.

National Category
Biological Sciences
Identifiers
urn:nbn:se:umu:diva-144802 (URN)1752-9867 (Electronic) 1674-2052 (Linking) (ISBN)
Note

Wang, Fei Qi, Yafei Malnoe, Alizee Choquet, Yves Wollman, Francis-Andre de Vitry, Catherine ENG England 2016/10/06 06:00 Mol Plant. 2016 Oct 1. pii: S1674-2052(16)30221-0. doi: 10.1016/j.molp.2016.09.012.

Available from: 2018-02-17 Created: 2018-02-17 Last updated: 2018-06-09
Rappaport, F., Malnoë, A. & Govindjee, G. (2015). Gordon research conference on photosynthesis: from evolution of fundamental mechanisms to radical re-engineering. Photosynth Res, 123(2), 213-23
Open this publication in new window or tab >>Gordon research conference on photosynthesis: from evolution of fundamental mechanisms to radical re-engineering
2015 (English)In: Photosynth Res, Vol. 123, no 2, p. 213-23Article in journal (Refereed) Published
Abstract [en]

We provide here a News Report on the 2014 Gordon Research Conference on Photosynthesis, with the subtitle "From Evolution of Fundamental Mechanisms to Radical Re-Engineering." It was held at Mount Snow Resort, West Dover, Vermont, during August 10-15, 2014. After the formal sessions ended, four young scientists (Ute Ambruster of USA; Han Bao of USA; Nicoletta Liguori of the Netherlands; and Anat Shperberg-Avni of Israel) were recognized for their research; they each received a book from one of us (G) in memory of Colin A. Wraight (1945-2014), a brilliant and admired scientist who had been very active in the bioenergetics field in general and in past Gordon Conferences in particular, having chaired the 1988 Gordon Conference on Photosynthesis. (See an article on Wraight by one of us (Govindjee) at http://www.life.illinois.edu/plantbio/Features/ColinWraight/ColinWraight.html .).

National Category
Biological Sciences
Identifiers
urn:nbn:se:umu:diva-144803 (URN)1573-5079 (Electronic) 0166-8595 (Linking) (ISBN)
Note

Rappaport, Fabrice Malnoe, Alizee Govindjee eng News Netherlands 2014/11/27 06:00 Photosynth Res. 2015 Feb;123(2):213-23. doi: 10.1007/s11120-014-0058-9. Epub 2014 Nov 26.

Available from: 2018-02-17 Created: 2018-02-17 Last updated: 2018-06-09
Dent, R. M., Sharifi, M. N., Malnoë, A., Haglund, C., Calderon, R. H., Wakao, S. & Niyogi, K. K. (2015). Large-scale insertional mutagenesis of Chlamydomonas supports phylogenomic functional prediction of photosynthetic genes and analysis of classical acetate-requiring mutants. Plant J, 82(2), 337-51
Open this publication in new window or tab >>Large-scale insertional mutagenesis of Chlamydomonas supports phylogenomic functional prediction of photosynthetic genes and analysis of classical acetate-requiring mutants
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2015 (English)In: Plant J, Vol. 82, no 2, p. 337-51Article in journal (Refereed) Published
Abstract [en]

Chlamydomonas reinhardtii is a unicellular green alga that is a key model organism in the study of photosynthesis and oxidative stress. Here we describe the large-scale generation of a population of insertional mutants that have been screened for phenotypes related to photosynthesis and the isolation of 459 flanking sequence tags from 439 mutants. Recent phylogenomic analysis has identified a core set of genes, named GreenCut2, that are conserved in green algae and plants. Many of these genes are likely to be central to the process of photosynthesis, and they are over-represented by sixfold among the screened insertional mutants, with insertion events isolated in or adjacent to 68 of 597 GreenCut2 genes. This enrichment thus provides experimental support for functional assignments based on previous bioinformatic analysis. To illustrate one of the uses of the population, a candidate gene approach based on genome position of the flanking sequence of the insertional mutant CAL027_01_20 was used to identify the molecular basis of the classical C. reinhardtii mutation ac17. These mutations were shown to affect the gene PDH2, which encodes a subunit of the plastid pyruvate dehydrogenase complex. The mutants and associated flanking sequence data described here are publicly available to the research community, and they represent one of the largest phenotyped collections of algal insertional mutants to date.

Keywords
Chlamydomonas reinhardtii, GreenCut, Pdh2, genomics, insertion mutant, oxidative stress, photosynthesis
National Category
Biological Sciences
Identifiers
urn:nbn:se:umu:diva-144804 (URN)1365-313X (Electronic) 0960-7412 (Linking) (ISBN)
Note

Dent, Rachel M Sharifi, Marina N Malnoe, Alizee Haglund, Cat Calderon, Robert H Wakao, Setsuko Niyogi, Krishna K eng England 2015/02/26 06:00 Plant J. 2015 Apr;82(2):337-51. doi: 10.1111/tpj.12806.

Available from: 2018-02-17 Created: 2018-02-17 Last updated: 2018-06-09
Sylak-Glassman, E. J., Malnoë, A., De Re, E., Brooks, M. D., Fischer, A. L., Niyogi, K. K. & Fleming, G. R. (2014). Distinct roles of the photosystem II protein PsbS and zeaxanthin in the regulation of light harvesting in plants revealed by fluorescence lifetime snapshots. Proc Natl Acad Sci USA, 111(49), 17498-503
Open this publication in new window or tab >>Distinct roles of the photosystem II protein PsbS and zeaxanthin in the regulation of light harvesting in plants revealed by fluorescence lifetime snapshots
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2014 (English)In: Proc Natl Acad Sci USA, Vol. 111, no 49, p. 17498-503Article in journal (Refereed) Published
Abstract [en]

The photosystem II (PSII) protein PsbS and the enzyme violaxanthin deepoxidase (VDE) are known to influence the dynamics of energy-dependent quenching (qE), the component of nonphotochemical quenching (NPQ) that allows plants to respond to fast fluctuations in light intensity. Although the absence of PsbS and VDE has been shown to change the amount of quenching, there have not been any measurements that can detect whether the presence of these proteins alters the type of quenching that occurs. The chlorophyll fluorescence lifetime probes the excited-state chlorophyll relaxation dynamics and can be used to determine the amount of quenching as well as whether two different genotypes with the same amount of NPQ have similar dynamics of excited-state chlorophyll relaxation. We measured the fluorescence lifetimes on whole leaves of Arabidopsis thaliana throughout the induction and relaxation of NPQ for wild type and the qE mutants, npq4, which lacks PsbS; npq1, which lacks VDE and cannot convert violaxanthin to zeaxanthin; and npq1 npq4, which lacks both VDE and PsbS. These measurements show that although PsbS changes the amount of quenching and the rate at which quenching turns on, it does not affect the relaxation dynamics of excited chlorophyll during quenching. In addition, the data suggest that PsbS responds not only to DeltapH but also to the Deltapsi across the thylakoid membrane. In contrast, the presence of VDE, which is necessary for the accumulation of zeaxanthin, affects the excited-state chlorophyll relaxation dynamics.

Keywords
Arabidopsis/enzymology, Arabidopsis Proteins/*metabolism, Chlorophyll/chemistry, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant, Genes, Plant/genetics, *Light, Light-Harvesting Protein Complexes/*metabolism, Oxidoreductases/metabolism, Photosystem II Protein Complex/*metabolism, Zeaxanthins/*metabolism, PsbS, carotenoids, fluorescence lifetime, nonphotochemical quenching, photosystem II
National Category
Biological Sciences
Identifiers
urn:nbn:se:umu:diva-144806 (URN)1091-6490 (Electronic) 0027-8424 (Linking) (ISBN)
Note

Sylak-Glassman, Emily J Malnoe, Alizee De Re, Eleonora Brooks, Matthew D Fischer, Alexandra Lee Niyogi, Krishna K Fleming, Graham R eng Howard Hughes Medical Institute/ Research Support, Non-U.S. Gov't 2014/11/26 06:00 Proc Natl Acad Sci U S A. 2014 Dec 9;111(49):17498-503. doi: 10.1073/pnas.1418317111. Epub 2014 Nov 24.

Available from: 2018-02-17 Created: 2018-02-17 Last updated: 2018-06-09
Wei, L., Derrien, B., Gautier, A., Houille-Vernes, L., Boulouis, A., Saint-Marcoux, D., . . . Wollman, F. A. (2014). Nitric oxide-triggered remodeling of chloroplast bioenergetics and thylakoid proteins upon nitrogen starvation in Chlamydomonas  reinhardtii. Plant Cell, 26(1), 353-72
Open this publication in new window or tab >>Nitric oxide-triggered remodeling of chloroplast bioenergetics and thylakoid proteins upon nitrogen starvation in Chlamydomonas  reinhardtii
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2014 (English)In: Plant Cell, Vol. 26, no 1, p. 353-72Article in journal (Refereed) Published
Abstract [en]

Starving microalgae for nitrogen sources is commonly used as a biotechnological tool to boost storage of reduced carbon into starch granules or lipid droplets, but the accompanying changes in bioenergetics have been little studied so far. Here, we report that the selective depletion of Rubisco and cytochrome b6f complex that occurs when Chlamydomonas reinhardtii is starved for nitrogen in the presence of acetate and under normoxic conditions is accompanied by a marked increase in chlororespiratory enzymes, which converts the photosynthetic thylakoid membrane into an intracellular matrix for oxidative catabolism of reductants. Cytochrome b6f subunits and most proteins specifically involved in their biogenesis are selectively degraded, mainly by the FtsH and Clp chloroplast proteases. This regulated degradation pathway does not require light, active photosynthesis, or state transitions but is prevented when respiration is impaired or under phototrophic conditions. We provide genetic and pharmacological evidence that NO production from intracellular nitrite governs this degradation pathway: Addition of a NO scavenger and of two distinct NO producers decrease and increase, respectively, the rate of cytochrome b6f degradation; NO-sensitive fluorescence probes, visualized by confocal microscopy, demonstrate that nitrogen-starved cells produce NO only when the cytochrome b6f degradation pathway is activated.

Keywords
Chlamydomonas reinhardtii/*metabolism/physiology/ultrastructure, Cytochrome b6f Complex/genetics/metabolism, Energy Metabolism, Nitric Oxide/metabolism/*pharmacology, Nitrites/metabolism, Nitrogen/*metabolism, Photosynthesis, Proteolysis, Ribulose-Bisphosphate Carboxylase/genetics/metabolism, Thylakoids/*metabolism
National Category
Biological Sciences
Identifiers
urn:nbn:se:umu:diva-144805 (URN)1532-298X (Electronic) 1040-4651 (Linking) (ISBN)
Note

Wei, Lili Derrien, Benoit Gautier, Arnaud Houille-Vernes, Laura Boulouis, Alix Saint-Marcoux, Denis Malnoe, Alizee Rappaport, Fabrice de Vitry, Catherine Vallon, Olivier Choquet, Yves Wollman, Francis-Andre eng Research Support, Non-U.S. Gov't 2014/01/30 06:00 Plant Cell. 2014 Jan;26(1):353-72. doi: 10.1105/tpc.113.120121. Epub 2014 Jan 28.

Available from: 2018-02-17 Created: 2018-02-17 Last updated: 2018-06-09
Malnoë, A., Wang, F., Girard-Bascou, J., Wollman, F. A. & de Vitry, C. (2014). Thylakoid FtsH protease contributes to photosystem II and cytochrome b6f remodeling in Chlamydomonas  reinhardtii under stress conditions. Plant Cell, 26(1), 373-90
Open this publication in new window or tab >>Thylakoid FtsH protease contributes to photosystem II and cytochrome b6f remodeling in Chlamydomonas  reinhardtii under stress conditions
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2014 (English)In: Plant Cell, Vol. 26, no 1, p. 373-90Article in journal (Refereed) Published
Abstract [en]

FtsH is the major thylakoid membrane protease found in organisms performing oxygenic photosynthesis. Here, we show that FtsH from Chlamydomonas reinhardtii forms heterooligomers comprising two subunits, FtsH1 and FtsH2. We characterized this protease using FtsH mutants that we identified through a genetic suppressor approach that restored phototrophic growth of mutants originally defective for cytochrome b6f accumulation. We thus extended the spectrum of FtsH substrates in the thylakoid membranes beyond photosystem II, showing the susceptibility of cytochrome b6f complexes (and proteins involved in the ci heme binding pathway to cytochrome b6) to FtsH. We then show how FtsH is involved in the response of C. reinhardtii to macronutrient stress. Upon phosphorus starvation, photosynthesis inactivation results from an FtsH-sensitive photoinhibition process. In contrast, we identified an FtsH-dependent loss of photosystem II and cytochrome b6f complexes in darkness upon sulfur deprivation. The D1 fragmentation pattern observed in the latter condition was similar to that observed in photoinhibitory conditions, which points to a similar degradation pathway in these two widely different environmental conditions. Our experiments thus provide extensive evidence that FtsH plays a major role in the quality control of thylakoid membrane proteins and in the response of C. reinhardtii to light and macronutrient stress.

Keywords
ATP-Dependent Proteases/genetics/metabolism/*physiology, Algal Proteins/genetics/metabolism/*physiology, Chlamydomonas reinhardtii/*enzymology/genetics/metabolism, Cloning, Molecular, Cytochrome b6f Complex/*metabolism, Photosystem II Protein Complex/*metabolism, Point Mutation, *Stress, Physiological, Thylakoids/*metabolism
National Category
Biological Sciences
Identifiers
urn:nbn:se:umu:diva-144807 (URN)1532-298X (Electronic) 1040-4651 (Linking) (ISBN)
Note

Malnoe, Alizee Wang, Fei Girard-Bascou, Jacqueline Wollman, Francis-Andre de Vitry, Catherine eng Research Support, Non-U.S. Gov't 2014/01/23 06:00 Plant Cell. 2014 Jan;26(1):373-90. doi: 10.1105/tpc.113.120113. Epub 2014 Jan 21.

Available from: 2018-02-17 Created: 2018-02-17 Last updated: 2018-06-09
Calderon, R. H., Garcia-Cerdan, J. G., Malnoë, A., Cook, R., Russell, J. J., Gaw, C., . . . Niyogi, K. K. (2013). A conserved rubredoxin is necessary for photosystem II accumulation in diverse oxygenic photoautotrophs. J Biol Chem, 288(37), 26688-96
Open this publication in new window or tab >>A conserved rubredoxin is necessary for photosystem II accumulation in diverse oxygenic photoautotrophs
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2013 (English)In: J Biol Chem, Vol. 288, no 37, p. 26688-96Article in journal (Refereed) Published
Abstract [en]

In oxygenic photosynthesis, two photosystems work in tandem to harvest light energy and generate NADPH and ATP. Photosystem II (PSII), the protein-pigment complex that uses light energy to catalyze the splitting of water, is assembled from its component parts in a tightly regulated process that requires a number of assembly factors. The 2pac mutant of the unicellular green alga Chlamydomonas reinhardtii was isolated and found to have no detectable PSII activity, whereas other components of the photosynthetic electron transport chain, including photosystem I, were still functional. PSII activity was fully restored by complementation with the RBD1 gene, which encodes a small iron-sulfur protein known as a rubredoxin. Phylogenetic evidence supports the hypothesis that this rubredoxin and its orthologs are unique to oxygenic phototrophs and distinct from rubredoxins in Archaea and bacteria (excluding cyanobacteria). Knockouts of the rubredoxin orthologs in the cyanobacterium Synechocystis sp. PCC 6803 and the plant Arabidopsis thaliana were also found to be specifically affected in PSII accumulation. Taken together, our data suggest that this rubredoxin is necessary for normal PSII activity in a diverse set of organisms that perform oxygenic photosynthesis.

Keywords
Amino Acid Sequence, Arabidopsis/metabolism, Chlamydomonas reinhardtii/metabolism, Chlorophyll/chemistry, Conserved Sequence, *Gene Expression Regulation, Bacterial, *Gene Expression Regulation, Enzymologic, *Gene Expression Regulation, Plant, Genetic Complementation Test, Molecular Sequence Data, Mutation, Phenotype, Photosynthesis, Photosystem II Protein Complex/*metabolism, Phylogeny, Rubredoxins/*chemistry/genetics, Seeds/metabolism, Species Specificity, Spectrophotometry, Synechocystis/metabolism, Arabidopsis, Chlamydomonas, Chloroplast, Electron transport, Iron-sulfur protein, Photosystem II, Rubredoxin, Synechocystis
National Category
Biological Sciences
Identifiers
urn:nbn:se:umu:diva-144808 (URN)1083-351X (Electronic) 0021-9258 (Linking) (ISBN)
Note

Calderon, Robert H Garcia-Cerdan, Jose G Malnoe, Alizee Cook, Ron Russell, James J Gaw, Cynthia Dent, Rachel M de Vitry, Catherine Niyogi, Krishna K eng Howard Hughes Medical Institute/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. 2013/08/01 06:00 J Biol Chem. 2013 Sep 13;288(37):26688-96. doi: 10.1074/jbc.M113.487629. Epub 2013 Jul 30.

Available from: 2018-02-17 Created: 2018-02-17 Last updated: 2018-06-09
Malnoë, A., Wollman, F. A., de Vitry, C. & Rappaport, F. (2011). Photosynthetic growth despite a broken Q-cycle. Nat Commun, 2, 301-306
Open this publication in new window or tab >>Photosynthetic growth despite a broken Q-cycle
2011 (English)In: Nat Commun, Vol. 2, p. 301-306Article 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.

Keywords
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:nbn:se:umu:diva-144809 (URN)2041-1723 (Electronic) 2041-1723 (Linking) (ISBN)
Note

Malnoe, Alizee Wollman, Francis-Andre de Vitry, Catherine Rappaport, Fabrice eng Research Support, Non-U.S. Gov't England 2011/05/11 06:00 Nat Commun. 2011;2:301. doi: 10.1038/ncomms1299.

Available from: 2018-02-14 Created: 2018-02-14 Last updated: 2018-06-09
Projects
Molecular Mechanisms of Photoprotection in Plants [2018-04150_VR]; Umeå University
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0002-8777-3174

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