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[FeFe]-hydrogenases as biocatalysts in bio-hydrogen production

Morra, Simone; Valetti, Francesca; Gilardi, Gianfranco

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Authors

Profile image of SIMONE MORRA

SIMONE MORRA SIMONE.MORRA@NOTTINGHAM.AC.UK
Assistant Professor in Chemical &environmental Engineering

Francesca Valetti

Gianfranco Gilardi



Abstract

© 2016, Accademia Nazionale dei Lincei. [FeFe]-hydrogenases catalyse H2 production at exceptionally high turnover numbers (up to 104s−1). They are found in a variety of strict or facultative anaerobic microorganisms, such as bacteria of the genus Clostridium, Desulfovibrio, Thermotoga, and eukaryotes ranging from unicellular and coenobial green algae to anaerobic fungi, ciliates and trichomonads. Key to their activity is an organometallic centre, the H-cluster that cooperates tightly with the protein framework to reduce two protons into molecular hydrogen. The assembly of the catalytic site requires a specialised cellular mechanism based on the action of three other enzymes, called maturases: HydE, HydF and HydG. Recent advancements in the recombinant production of [FeFe]-hydrogenases have provided leaps forward in their exploitation in H2 production for clean energy storage. [FeFe]-hydrogenases have been used in several fermentative approaches where microorganisms are engineered to overexpress specific [FeFe]-hydrogenases to convert low-cost materials (e.g. wastes) into H2. [FeFe]-hydrogenases have also been proven to be excellent catalysts in different in vitro devices that can produce hydrogen directly from water, either via water electrolysis or via light-driven mechanisms, thus allowing the direct storage of solar energy into H2.

Citation

Morra, S., Valetti, F., & Gilardi, G. (2017). [FeFe]-hydrogenases as biocatalysts in bio-hydrogen production. Rendiconti Lincei, 28(S1), 183-194. https://doi.org/10.1007/s12210-016-0584-9

Journal Article Type Article
Acceptance Date Nov 17, 2016
Online Publication Date Nov 24, 2016
Publication Date Jul 1, 2017
Deposit Date Jan 31, 2020
Publicly Available Date May 6, 2020
Journal Rendiconti Lincei
Print ISSN 2037-4631
Electronic ISSN 1720-0776
Publisher Springer Verlag
Peer Reviewed Peer Reviewed
Volume 28
Issue S1
Pages 183-194
DOI https://doi.org/10.1007/s12210-016-0584-9
Public URL https://nottingham-repository.worktribe.com/output/3841105
Publisher URL https://link.springer.com/article/10.1007/s12210-016-0584-9

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