Engineering the Electron Relay in [FeFe]-Hydrogenase Enhances Electrocatalytic H 2 Evolution

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Abstract
H2 is an ideal energy vector, but catalysts for its clean production from water are inefficient or expensive. [FeFe]-hydrogenases are the most active H2-converting catalysts in nature, using a unique organometallic active site finely tuned by the protein matrix. M3 type [FeFe]-hydrogenases from Clostridium pasteurianum and Clostridium acetobutylicum are exceptionally active for H2 production, and less O2 sensitive than most other types of [FeFe]-hydrogenases, making them attractive targets for biotechnology. However, they are more challenging to work with because of their large size and the number of iron–sulfur clusters. Here, the [FeFe]-hydrogenase from C. acetobutylicum was systematically engineered to truncate each iron–sulfur-containing region of the F-domain, yielding smaller and easier-to-produce catalytic systems. Detailed characterization revealed that these variants retain high electrocatalytic performance and other essential properties of the natural enzyme.
Funding Information
  • Engineering and Physical Sciences Research Council (EP/L011972/1, EP/V036408/1)
  • Royal Society (RGS\R1\231433)
  • John Fell Fund, University of Oxford (0007019)
  • Linacre College, University of Oxford
  • University of Leicester
  • University of Nottingham
  • Royal Society of Chemistry (R23-6753486967)
  • University of Oxford
  • H2020 European Research Council (819580)
  • Biotechnology and Biological Sciences Research Council (BB/X002624/1)

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