2015
DOI: 10.1104/pp.15.00105
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Induction of Photosynthetic Carbon Fixation in Anoxia Relies on Hydrogenase Activity and Proton-Gradient Regulation-Like1-Mediated Cyclic Electron Flow in Chlamydomonas reinhardtii

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Cited by 61 publications
(61 citation statements)
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“…In addition, TOR‐inhibited cells exhibited adverse effects on electron transport rate (ETR PSII ) parameter as well where ETR PSII showed significant drop by 4, 8, and 12 hr of TOR kinase inhibition (Figure c). We note that in the same experiment, control untreated cells exhibited ETR PSII values that were similar to the previously reported values (Godaux, Bailleul, Berne, & Cardol, ). Thus, our studies indicate that TOR inhibition causes significant loss in chloroplast function, which is also reflected by alterations in chloroplast morphology.…”
Section: Resultssupporting
confidence: 91%
“…In addition, TOR‐inhibited cells exhibited adverse effects on electron transport rate (ETR PSII ) parameter as well where ETR PSII showed significant drop by 4, 8, and 12 hr of TOR kinase inhibition (Figure c). We note that in the same experiment, control untreated cells exhibited ETR PSII values that were similar to the previously reported values (Godaux, Bailleul, Berne, & Cardol, ). Thus, our studies indicate that TOR inhibition causes significant loss in chloroplast function, which is also reflected by alterations in chloroplast morphology.…”
Section: Resultssupporting
confidence: 91%
“…This is in agreement with the proposal that PQH 2 replaces PhQ in the A 1 site of PSI in anoxia and prevents photosynthetic electron transfer in the mend mutant (McConnell et al ., ). As a result, long‐term reactivation (>5 min) of PSII electron transfer in anoxia, which relies on both PSI‐dependent hydrogenase activity and PGRL1‐dependent PSI cyclic electron flow in wild‐type Chlamydomonas cells (Godaux et al ., ), is fully compromised in the men mutant (Figure b). Loss of PhQ thus severely impairs electron transfer in anoxia in our men mutants, as has already been shown in the mend mutant (Lefebvre‐Legendre et al ., ; McConnell et al ., ).…”
Section: Discussionmentioning
confidence: 92%
“…The ratio between active PSI and PSII centers was estimated as previously described (Godaux et al ., ) on cells adapted to the dark for 30 min. Briefly, the amplitude of the fast phase (<1 ms) of the ECS signal (at 520–546 nm) after illumination with a single‐turnover laser flash was monitored with a JTS‐10 spectrophotometer (Bio‐Logic).…”
Section: Methodsmentioning
confidence: 99%
“…Maturation of the [FeFe]‐hydrogenase requires HydE, HydF and HydG maturation factors. The [FeFe]‐hydrogenase maturation factors (maturase) were first identified in the green alga Chlamydomonas , while the HydE and HydF are fused to form one protein HydEF in Chlamydomonas , and hydrogen evolution was barely detected in the hydEF‐1 mutant, as well as hydG‐1 and hydG‐2 mutants . The HydEF and HydG are all hydrogenase maturation factors, while the distinctions between HydEF and HydG have not been revealed in Chlamydomonas .…”
Section: Hydrogen Synthesizing Enzymes In Microalgaementioning
confidence: 99%
“…The [FeFe]-hydrogenase maturation factors (maturase) were first identified in the green alga Chlamydomonas, while the HydE and HydF are fused to form one protein HydEF in Chlamydomonas, and hydrogen evolution was barely detected in the hydEF-1 mutant, [46] as well as hydG-1 [90] and hydG-2 mutants. [91] The HydEF and HydG are all hydrogenase maturation factors, while the distinctions between HydEF and HydG have not been revealed in Chlamydomonas. In vivo, when [FeFe]-hydrogenase was expressed in E. coli without maturase, an inactive protein lacking H-cluster was generated, [92] and the subsequent evidences indicated that active H-cluster is responsible for the 10-100 folds higher activity of [FeFe]hydrogenase than that of [NiFe]-hydrogenase.…”
Section: The Maturation Of [Fefe]-hydrogenasementioning
confidence: 99%