4.6 Article

Semi-synthetic hydrogenases-in vitro and in vivo applications

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DOI: 10.1016/j.cogsc.2021.100521

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  1. Novo Nordisk Foundation [NNF19OC0055613]
  2. European Research Council [714102]
  3. European Research Council (ERC) [714102] Funding Source: European Research Council (ERC)

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Hydrogenases are crucial enzymes central in hydrogen metabolism, and the semi-synthetic approach has helped to elucidate their structure, function, biodiversity, and catalytic mechanisms. Additionally, investigating the assembly line of these enzymes using synthetic precursors provides detailed insight into their biosynthesis process.
Hydrogenases are gas processing redox enzymes central in hydrogen metabolism. The interdisciplinary nature of hydrogenase research is underscored by the development of artificial maturation, enabling the preparation of semi-synthetic hydrogenases through the incorporation of synthetic cofactors into a range of apo-hydrogenase hosts under in vitro and in vivo conditions. Herein, we discuss how the preparation of such semi-synthetic [FeFe]-hydrogenases has elucidated structural elements of the cofactor critical for catalysis and reactivity towards known inhibitors. It has also provided a convenient method for exploring the biodiversity of this enzyme family and thereby facilitated investigation of the role of the outer-coordination sphere in tuning the reactivity of the H-cluster. In parallel, hijacking the assembly line of the [FeFe]-hydrogenase through incorporation of synthetic precursors has provided detailed insight into the biosynthesis of the H-cluster. Moreover, it has allowed the preparation of Mn analogs of [Fe] hydrogenase.

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