ArticleProceedings of the National Academy of Sciences of the United States of America2011
Plastid terminal oxidase 2 (PTOX2) is the major oxidase involved in chlororespiration in Chlamydomonas.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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73 citing papers in PubMed, 171 citations in OpenAlex.
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- Chlamydomonas mutants lacking chloroplast TRIOSE PHOSPHATE TRANSPORTER3 are metabolically compromised and light sensitive.The Plant cell · 2023Article
- Restricting electron flow at cytochrome b6f when downstream electron acceptors are severely limited.Plant physiology · 2023Article
- One-helix protein 2 is not required for the synthesis of photosystem II subunit D1 in Chlamydomonas.Plant physiology · 2023Article
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- Plastoquinone pool redox state and control of state transitions in Chlamydomonas reinhardtii in darkness and under illumination.Photosynthesis research · 2023Article
- Characterization of the wave phenomenon of flash-induced chlorophyll fluorescence in Chlamydomonas reinhardtii.Photosynthesis research · 2022Article
- Characterization of the Wave Phenomenon in Flash-Induced Fluorescence Relaxation and Its Application to Study Cyclic Electron Pathways in Microalgae.International journal of molecular sciences · 2022Article
- PTOX-dependent safety valve does not oxidize P700 during photosynthetic induction in the Arabidopsis pgr5 mutant.Plant physiology · 2022Article
- Evaluation of visible-light wavelengths that reduce or oxidize the plastoquinone pool in green algae with the activated FPhotosynthetica · 2022Article
- Distinct roles of alternative oxidase pathway during the greening process of etiolated algae.Science China. Life sciences · 2021Article
13 more citing papers are in PubMed but not listed here.
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
By homology with the unique plastid terminal oxidase (PTOX) found in plants, two genes encoding oxidases have been found in the Chlamydomonas genome, PTOX1 and PTOX2. Here we report the identification of a knockout mutant of PTOX2. Its molecular and functional characterization demonstrates that it encodes the oxidase most predominantly involved in chlororespiration in this algal species. In this mutant, the plastoquinone pool is constitutively reduced under dark-aerobic conditions, resulting in the mobile light-harvesting complexes being mainly, but reversibly, associated with photosystem I. Accordingly, the ptox2 mutant shows lower fitness than wild type when grown under phototrophic conditions. Single and double mutants devoid of the cytochrome b(6)f complex and PTOX2 were used to measure the oxidation rates of plastoquinols via PTOX1 and PTOX2. Those lacking both the cytochrome b(6)f complex and PTOX2 were more sensitive to light than the single mutants lacking either the cytochrome b(6)f complex or PTOX2, which discloses the role of PTOX2 under extreme conditions where the plastoquinone pool is overreduced. A model for chlororespiration is proposed to relate the electron flow rate through these alternative pathways and the redox state of plastoquinones in the dark. This model suggests that, in green algae and plants, the redox poise results from the balanced accumulation of PTOX and NADPH dehydrogenase.
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