ArticleScientific reports2015
Lyophilization protects [FeFe]-hydrogenases against O2-induced H-cluster degradation.
Article in Scientific reports, 2015. 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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Who cites it
10 citing papers in PubMed, 29 citations in OpenAlex.
- Hydride state accumulation in native [FeFe]-hydrogenase with the physiological reductant HChemical communications (Cambridge, England) · 2022Article
- Spontaneous assembly of redox-active iron-sulfur clusters at low concentrations of cysteine.Nature communications · 2021Article
- A safety cap protects hydrogenase from oxygen attack.Nature communications · 2021Article
- [FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- The final steps of [FeFe]-hydrogenase maturation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases.Nature communications · 2018Article
- From protein engineering to artificial enzymes - biological and biomimetic approaches towards sustainable hydrogen production.Sustainable energy & fuels · 2018Review
- Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases.Nature communications · 2017Article
- Mechanism of ONature chemistry · 2017Article
- Vibrational spectroscopy reveals the initial steps of biological hydrogen evolution.Chemical science · 2016Article
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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
Nature has developed an impressive repertoire of metal-based enzymes that perform complex chemical reactions under moderate conditions. Catalysts that produce molecular hydrogen (H2) are particularly promising for renewable energy applications. Unfortunately, natural and chemical H2-catalysts are often irreversibly degraded by molecular oxygen (O2). Here we present a straightforward procedure based on freeze-drying (lyophilization), that turns [FeFe]-hydrogenases, which are excellent H2-producers, but typically extremely O2-sensitive in solution, into enzymes that are fully resistant against O2. Complete dryness protects and conserves both, the [FeFe]-hydrogenase proteins and their inorganic active-site cofactor (H-cluster), when exposed to 100% O2 for days. The full H2-formation capacity is restored after solvation of the lyophilized enzymes. However, even minimal moisturizing re-establishes O2-sensitivity. The dry [FeFe]-hydrogenase material is superior also for advanced spectroscopic investigations on the H-cluster reaction mechanism. Our method provides a convenient way for long-term storage and impacts on potential biotechnological hydrogen production applications of hydrogenase enzymes.
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