ArticlePhotosynthesis research2016
Crystal structure and biochemical characterization of Chlamydomonas FDX2 reveal two residues that, when mutated, partially confer FDX2 the redox potential and catalytic properties of FDX1.
Article in Photosynthesis research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 30 citations in OpenAlex.
- Client distribution between Chlamydomonas FDX1 and FDX2 in carbon, nitrogen and sulfur assimilation.bioRxiv : the preprint server for biology · 2026Article
- Characteristics of RecombinantJournal of microbiology and biotechnology · 2024Article
- The AlgaInternational journal of molecular sciences · 2023Article
- Changing the tracks: screening for electron transfer proteins to support hydrogen production.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- CP12 fine-tunes the Calvin-Benson cycle and carbohydrate metabolism in cyanobacteria.Frontiers in plant science · 2022Article
- Fine-tuning of FeS proteins monitored via pulsed EPR redox potentiometry at Q-band.Biophysical reports · 2021Article
- The structure and reactivity of the HoxEFU complex from the cyanobacteriumThe Journal of biological chemistry · 2020Article
- Ferredoxin5 Deletion Affects Metabolism of Algae during the Different Phases of Sulfur Deprivation.Plant physiology · 2019Article
- Association of Ferredoxin:NADPPhotosynthesis research · 2017Article
- Evolution of Chlamydomonas reinhardtii ferredoxins and their interactions with [FeFe]-hydrogenases.Photosynthesis research · 2017Review
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The green alga Chlamydomonas reinhardtii contains six plastidic [2Fe2S]-cluster ferredoxins (FDXs), with FDX1 as the predominant isoform under photoautotrophic growth. FDX2 is highly similar to FDX1 and has been shown to interact with specific enzymes (such as nitrite reductase), as well as to share interactors with FDX1, such as the hydrogenases (HYDA), ferredoxin:NAD(P) reductase I (FNR1), and pyruvate:ferredoxin oxidoreductase (PFR1), albeit performing at low catalytic rates. Here we report the FDX2 crystal structure solved at 1.18 Å resolution. Based on differences between the Chlorella fusca FDX1 and C. reinhardtii FDX2 structures, we generated and purified point-mutated versions of the FDX2 protein and assayed them in vitro for their ability to catalyze hydrogen and NADPH photo-production. The data show that structural differences at two amino acid positions contribute to functional differences between FDX1 and FDX2, suggesting that FDX2 might have evolved from FDX1 toward a different physiological role in the cell. Moreover, we demonstrate that the mutations affect both the midpoint potentials of the FDX and kinetics of the FNR reaction, possibly due to altered binding between FDX and FNR. An effect on H2 photo-production rates was also observed, although the kinetics of the reaction were not further characterized.
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