Co-expression of auxiliary genes enhances the activity of a heterologous O2-tolerant hydrogenase in the cyanobacterium Synechocystis sp. PCC 6803
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Abstract Cyanobacteria bear great biotechnological potential as photosynthetic cell factories. In particular, hydrogenases are promising with respect to light-driven H 2 production as well as H 2 -driven redox biocatalysis. Their utilization relies on effective strain design as well as a balanced synthesis and maturation of heterologous enzymes. In a previous study, the soluble O 2 -tolerant hydrogenase complex from Cupriavidus necator ( Cn SH) could be introduced into the model cyanobacterium Synechocystis sp. PCC 6803. Due to its O 2 -tolerance, it was indeed active under photoautotrophic growth conditions. However, the specific activity was rather low indicating that further engineering is required, for which we followed a two-step approach. First, we optimized the Cn SH multigene expression in Synechocystis by applying different regulatory elements. Although corresponding protein levels and specific Cn SH activity increased, the apparent rise in enzyme levels did not fully translate into activity increase. Second, the entire set of hyp genes, encoding Cn SH maturases, was co-expressed in Synechocystis to investigate, if Cn SH maturation was limiting. Indeed, the native Cn SH maturation apparatus promoted functional Cn SH synthesis, enabling a threefold higher H 2 oxidation activity compared to the parental strain. Our results suggest that a fine balance between heterologous hydrogenase and maturase expression is required to ensure high specific activity over an extended time period.
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Enzymes from different organisms can vary in their optimal temperatures, pH, cofactor dependencies, and protein-folding properties.
“Enzymes from different organisms can vary in their optimal temperatures, pH, cofactor dependencies, and protein-folding [primary, secondary, tertiary, or quaternary] properties [152].”
From Cyanobacteria as a Photosynthetic Chassis for Metabolic Pathway Engineering with Heterologous Gene Expression (2026) · cites this paper as [152]
The Discussion (page unavailable) says that producing functional hydrogenase in a different host can be difficult because maturation depends on compatible auxiliary proteins. That supports a narrower point about host-dependent enzyme maturation, but the paper does not establish the claimed variation in optimal temperature, pH, cofactor dependencies, or primary through quaternary protein-folding properties. (LLM, conf=0.83)
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- Authors
- Lupacchini, S., Stauder, R., Opel, F., Klähn, S., Schmid, A., Bühler, B., & Toepel, J.
- Affiliations
- Helmholtz Centre for Environmental Research (DE)
- Corresponding author
- Toepel, Jörg
- Venue
- Biotechnology for Biofuels and Bioproducts
- Published
- 2025-03-28
- Volume
- 18
- Issue
- 1
- Pages
- 41-41
- ISSN
- 2731-3654 (ISSN-L)
- PMC
- PMC11954184
- OpenAlex
- W4408969186
- Cited by
- 12
- References
- 74
- Citations by year
- 2026: 9 · 2025: 3
- FWCI
- 1.66
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Biotechnology for Biofuels and Bioproducts (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Helmholtz-Zentrum für Umweltforschung GmbH - UFZ
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Algal biology and biofuel production
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
- Keywords
- Synechocystis sp. PCC 6803, heterologous expression, hydrogenase maturation, hydrogen production, hydrogen oxidation, cyanobacteria, gene expression regulation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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