Evidence map›Paper›PMID 27582874›Full record

ArticleBiotechnology for biofuels2016

The dual effect of a ferredoxin-hydrogenase fusion protein in vivo: successful divergence of the photosynthetic electron flux towards hydrogen production and elevated oxygen tolerance.

Haviva Eilenberg, Iddo Weiner, Oren Ben-Zvi, Carmel Pundak, Abigail Marmari, Oded Liran, Matt S Wecker, Yuval Milrad, Iftach Yacoby

Open access · goldAbstract read
In one paragraph

Article in Biotechnology for biofuels, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.5field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed, 93 citations in OpenAlex.

  1. Structural proteomics reveals the functional docking interface of ferredoxin-NADPThe Plant journal : for cell and molecular biology · 2026
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  5. Light-Driven HPlants (Basel, Switzerland) · 2024
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  17. EngineeredBiotechnology for biofuels · 2019
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 3 countries.

Haviva Eilenberg *Department of Molecular Biology and Ecology of Plants, The George S. Wise Faculty of Life Science, Tel Aviv University, Ramat Aviv, 69978 Tel Aviv, Israel.
Iddo Weiner *Department of Molecular Biology and Ecology of Plants, The George S. Wise Faculty of Life Science, Tel Aviv University, Ramat Aviv, 69978 Tel Aviv, Israel.
Oren Ben-ZviDepartment of Molecular Biology and Ecology of Plants, The George S. Wise Faculty of Life Science, Tel Aviv University, Ramat Aviv, 69978 Tel Aviv, Israel.
Carmel PundakDepartment of Molecular Biology and Ecology of Plants, The George S. Wise Faculty of Life Science, Tel Aviv University, Ramat Aviv, 69978 Tel Aviv, Israel.
Abigail MarmariDepartment of Molecular Biology and Ecology of Plants, The George S. Wise Faculty of Life Science, Tel Aviv University, Ramat Aviv, 69978 Tel Aviv, Israel.
Oded LiranDepartment of Molecular Biology and Ecology of Plants, The George S. Wise Faculty of Life Science, Tel Aviv University, Ramat Aviv, 69978 Tel Aviv, Israel.
Matt S WeckerGeneBiologics, LLC, Boulder, CO USA.
Yuval MilradDepartment of Molecular Biology and Ecology of Plants, The George S. Wise Faculty of Life Science, Tel Aviv University, Ramat Aviv, 69978 Tel Aviv, Israel.
Iftach YacobyDepartment of Molecular Biology and Ecology of Plants, The George S. Wise Faculty of Life Science, Tel Aviv University, Ramat Aviv, 69978 Tel Aviv, Israel.ORCID 0000-0003-0177-0624
Tel Aviv University · ILNational Laboratory of the Rockies · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundHydrogen photo-production in green algae, catalyzed by the enzyme [FeFe]-hydrogenase (HydA), is considered a promising source of renewable clean energy. Yet, a significant increase in hydrogen production efficiency is necessary for industrial scale-up. We have previously shown that a major challenge to be resolved is the inferior competitiveness of HydA with NADPH production, catalyzed by ferredoxin-NADP(+)-reductase (FNR). In this work, we explored the in vivo hydrogen production efficiency of Fd-HydA, where the electron donor ferredoxin (Fd) is fused to HydA and expressed in the model organism Chlamydomonas reinhardtii.

resultsWe show that once the Fd-HydA fusion gene is expressed in micro-algal cells of C. reinhardtii, the fusion enzyme is able to intercept photosynthetic electrons and use them for efficient hydrogen production, thus supporting the previous observations made in vitro. We found that Fd-HydA has a ~4.5-fold greater photosynthetic hydrogen production rate standardized for hydrogenase amount (PHPRH) than that of the native HydA in vivo. Furthermore, we provide evidence suggesting that the fusion protein is more resistant to oxygen than the native HydA.

conclusionsThe in vivo photosynthetic activity of the Fd-HydA enzyme surpasses that of the native HydA and shows higher oxygen tolerance. Therefore, our results provide a solid platform for further engineering efforts towards efficient hydrogen production in microalgae through the expression of synthetic enzymes.

Indexed as

Chlamydomonas reinhardtiiFerredoxinFusion enzymeH2 productionHydrogenaseOxygen sensitivity

Identifiers

PMID27582874
PMCPMC5006448
OpenAlexW2512653639

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.