De novo metalloprotein design involves the construction of proteins guided by specific repeat patterns of polar and apolar residues, which, upon self‐assembly, provide a suitable environment to bind metals and produce artificial metalloenzymes. While a wide range of functionalities have been realized in de novo designed metalloproteins, the functional repertoire of such constructs towards alternative energy‐relevant catalysis is currently limited. Here we show the application of de novo approach to design a functional H2evolving protein. The design involved the assembly of an amphiphilic peptide featuring cysteines at tandem
Hydrogenase enzymes produce H2gas, which can be a potential source of alternative energy. Inspired by the [NiFe] hydrogenases, we report the construction of a de novo‐designed artificial hydrogenase (ArH). The ArH is a dimeric coiled coil where two cysteine (Cys) residues are introduced at tandem
- Award ID(s):
- 1757220
- NSF-PAR ID:
- 10224130
- Publisher / Repository:
- Wiley Blackwell (John Wiley & Sons)
- Date Published:
- Journal Name:
- ChemSusChem
- Volume:
- 14
- Issue:
- 10
- ISSN:
- 1864-5631
- Page Range / eLocation ID:
- p. 2237-2246
- Format(s):
- Medium: X
- Sponsoring Org:
- National Science Foundation
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