ArticleProceedings of the National Academy of Sciences of the United States of America2023
An expandable, modular de novo protein platform for precision redox engineering.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Emergence of specific binding and catalysis from a designed generalist binding protein.Nature chemistry · 2026Article
- Confinement and Catalysis withinJournal of the American Chemical Society · 2025Article
- De Novo design of α-helical heme binding proteins capable of versatile cofactor ligation.Methods in enzymology · 2025Article
- Development of artificial photosystems based on designed proteins for mechanistic insights into photosynthesis.Protein science : a publication of the Protein Society · 2024Review
- Computational design of de novo bioenergetic membrane proteins.Biochemical Society transactions · 2024Review
- Exo-chirality of the α-helix.Nature communications · 2024Article
- Delineating redox cooperativity in water-soluble and membrane multiheme cytochromes through protein design.Protein science : a publication of the Protein Society · 2024Article
- Fluctuation Relations to Calculate Protein Redox Potentials from Molecular Dynamics Simulations.Journal of chemical theory and computation · 2024Article
- Protein dynamics govern the oxyferrous state lifetime of an artificial oxygen transport protein.Biophysical journal · 2023Article
- An expandable, modular de novo protein platform for precision redox engineering.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
Corrections and comments
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Authors and funding
20 authors.
Funding
Abstract
The electron-conducting circuitry of life represents an as-yet untapped resource of exquisite, nanoscale biomolecular engineering. Here, we report the characterization and structure of a de novo diheme "maquette" protein, 4D2, which we subsequently use to create an expanded, modular platform for heme protein design. A well-folded monoheme variant was created by computational redesign, which was then utilized for the experimental validation of continuum electrostatic redox potential calculations. This demonstrates how fundamental biophysical properties can be predicted and fine-tuned. 4D2 was then extended into a tetraheme helical bundle, representing a 7 nm molecular wire. Despite a molecular weight of only 24 kDa, electron cryomicroscopy illustrated a remarkable level of detail, indicating the positioning of the secondary structure and the heme cofactors. This robust, expressible, highly thermostable and readily designable modular platform presents a valuable resource for redox protein design and the future construction of artificial electron-conducting circuitry.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.