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Hydrogen production by a fully de novo enzyme
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.ORCID iD: 0000-0003-3345-5602
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences, MMS, Medical Mass Spectrometry. Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.ORCID iD: 0000-0002-4062-7743
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2024 (English)Manuscript (preprint) (Other academic)
Abstract [en]

Molecular catalysts based on abundant elements that function in neutral water represent an essential component of sustainable hydrogen production. Artificial hydrogenases based on protein-inorganic hybrids have emerged as an intriguing class of catalysts for this purpose. We have prepared a novel artificial hydrogenase based on cobaloxime bound to a de novo three alpha-helical protein, α3C, via a pyridyl-based unnatural amino acid. The functionalized de novo protein was characterised by UV-visible, CD, and EPR spectroscopy, as well as MALDI spectrometry, which confirmed the presence and ligation of cobaloxime to the protein. The new de novo protein produced hydrogen under electrochemical, photochemical and reductive chemical conditions in neutral water solution. A change in hydrogen evolution capability of the de novo enzyme compared with native cobaloxime was observed, with turnover numbers around 80% of that of cobaloxime, and hydrogen evolution rates of 40% of that of cobaloxime. We discuss these findings in the context of existing literature, how our study contributes important information about the functionality of cobaloxime as hydrogen evolving catalysts in protein environments, and the feasibility of using de novo proteins for developent into artificial metalloenzymes. Small de novo proteins as enzyme scaffolds have the potential to function as upscalable bioinspired catalysts thanks to their efficient atom economy, and the findings presented here show that these types of novel enzymes are a possible product. 

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2024.
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URN: urn:nbn:se:uu:diva-526403OAI: oai:DiVA.org:uu-526403DiVA, id: diva2:1850357
Available from: 2024-04-10 Created: 2024-04-10 Last updated: 2024-04-10

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Berglund, SigridKaya, IbrahimAndrén, Per E.Shtender, VitaliiMagnuson, AnnGlover, Starla

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Berglund, SigridKaya, IbrahimAndrén, Per E.Shtender, VitaliiMagnuson, AnnGlover, Starla
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Physical ChemistryDepartment of Pharmaceutical BiosciencesMMS, Medical Mass SpectrometryDepartment of Medicinal ChemistryScience for Life Laboratory, SciLifeLabInorganic ChemistryApplied Material ScienceDepartment of Physical ChemistryMolecular BiomimeticsChemical PhysicsMolecular BiomimeticsMolecular Biomimetics
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