ArticleJournal of biological engineering2011
A synthetic system links FeFe-hydrogenases to essential E. coli sulfur metabolism.
Article in Journal of biological engineering, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 35 citations in OpenAlex.
- Using Domain Insertion to Create Sulfite Reductases That Present Chemical-Dependent Activities.ACS synthetic biology · 2026Article
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- On the emergence of metabolism: the evolution of proteins that powered life.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- Probing the Influence of the Protein Scaffold on H-Cluster Reactivity via Gain-of-Function Studies─Improved HJournal of the American Chemical Society · 2025Article
- A cellular selection identifies elongated flavodoxins that support electron transfer to sulfite reductase.Protein science : a publication of the Protein Society · 2023Article
- Article
- Thermodynamic Constraints on Electromicrobial Protein Production.Frontiers in bioengineering and biotechnology · 2022Article
- Article
- De novo design of symmetric ferredoxins that shuttle electrons in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Metalloprotein switches that display chemical-dependent electron transfer in cells.Nature chemical biology · 2019Article
- Evolutionary Relationships Between Low Potential Ferredoxin and Flavodoxin Electron Carriers.Frontiers in energy research · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundFeFe-hydrogenases are the most active class of H2-producing enzymes known in nature and may have important applications in clean H2 energy production. Many potential uses are currently complicated by a crucial weakness: the active sites of all known FeFe-hydrogenases are irreversibly inactivated by O2.
resultsWe have developed a synthetic metabolic pathway in E. coli that links FeFe-hydrogenase activity to the production of the essential amino acid cysteine. Our design includes a complementary host strain whose endogenous redox pool is insulated from the synthetic metabolic pathway. Host viability on a selective medium requires hydrogenase expression, and moderate O2 levels eliminate growth. This pathway forms the basis for a genetic selection for O2 tolerance. Genetically selected hydrogenases did not show improved stability in O2 and in many cases had lost H2 production activity. The isolated mutations cluster significantly on charged surface residues, suggesting the evolution of binding surfaces that may accelerate hydrogenase electron transfer.
conclusionsRational design can optimize a fully heterologous three-component pathway to provide an essential metabolic flux while remaining insulated from the endogenous redox pool. We have developed a number of convenient in vivo assays to aid in the engineering of synthetic H2 metabolism. Our results also indicate a H2-independent redox activity in three different FeFe-hydrogenases, with implications for the future directed evolution of H2-activating catalysts.
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Registered trials
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