Engineering the Electron Relay in [FeFe]-Hydrogenase Enhances Electrocatalytic H 2 Evolution
Year: 2025
Type: article
Abstract: High Resolution Image Download MS PowerPoint Slide H 2 is an ideal energy vector, but catalysts for its clean production from water are inefficient or expensive. [FeFe]-hydrogenases are the most active H 2 -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 H 2 production, and less O 2 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.
Source: ACS Catalysis
Authors: Tin Pou Lai, William K. Myers, Stephen B. Carr, Miguel A. Ramirez, Kylie A. Vincent, Simone Morra, Patricia Rodríguez-Maciá
Language: English
Field: Energy
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $4,500
Funders: University of Essex, Linacre College, University of Oxford, Royal Society, Royal Society of Chemistry, University of Leicester, University of Oxford, University of Nottingham, Directorate for Biological Sciences, Engineering and Physical Sciences Research Council, Biotechnology and Biological Sciences Research Council, John Fell Fund, University of Oxford, National Renewable Energy Laboratory, H2020 European Research Council
Awards: G157799150, G1836445909, G1991678457, G368544674, G3958972402, NextGen Structural Biology under Electrochemical Control: Filling in Missing Intermediates in Metalloenzyme Catalytic Cycles, Augmenting Oxford's Centre for Advanced Electron Spin Resonance with a Bruker Elexsys E580 X/Q-band pulsed ESR spectrometer, Biocatalysis for Sustainable Chemistry – Understanding Oxidation/Reduction of Small Molecules by Redox Metalloenzymes via a Suite of Steady State and Transient Infrared Electrochemical Methods, EPSRC Core Equipment Award 2020 - University of Oxford, G741436604
OpenAlex ID: W4415917973