Application of a synthetic ferredoxin‐inspired [4Fe4S]‐peptide maquette as the redox partner for a [FeFe]‐hydrogenase
‘Bacterial-type’ ferredoxins host a cubane [4Fe4S]2+/+ cluster that enables these proteins to mediate electron transfer and facilitate a broad range of biological processes. Peptide maquettes based on the conserved cluster-forming motif have previously been reported and used to model the ferredoxins. Herein we explore the integration of a [4Fe4S]-peptide maquette into a H2-powered electron transport chain. While routinely formed under anaerobic conditions, we illustrate by electron paramagnetic resonance (EPR) analysis that these maquettes can be reconstituted under aerobic conditions by using photoactivated NADH to reduce the cluster at 240 K. Attempts to tune the redox properties of the iron-sulfur cluster by introducing an Fe-coordinating selenocysteine residue were also explored. To demonstrate the integration of these artificial metalloproteins into a semi-synthetic electron transport chain, we utilize a ferredoxin-inspired [4Fe4S]-peptide maquette as the redox partner in the hydrogenase-mediated oxidation of H2.
Funding
Site-selective functionalisation of peptides and proteins via free-radical-induced dechalcogenation
Engineering and Physical Sciences Research Council
Find out more...Equipment to support Nottingham's Research Fellows
Engineering and Physical Sciences Research Council
Find out more...EPSRC National Electron Paramagnetic Resonance Facility and Service
Engineering and Physical Sciences Research Council
Find out more...A National Research Facility for EPR Spectroscopy, 2022-2027
Engineering and Physical Sciences Research Council
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School
- Aeronautical, Automotive, Chemical and Materials Engineering
Department
- Chemical Engineering
Published in
ChemBioChemVolume
24Issue
18Publisher
WileyVersion
- VoR (Version of Record)
Rights holder
© The AuthorsPublisher statement
This is an open access article under the terms of the Creative Commons Attribution (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.Acceptance date
2023-06-28Publication date
2023-08-13Copyright date
2023ISSN
1439-4227eISSN
1439-7633Publisher version
Language
- en