ArticleNature chemical biology2013
Elementary tetrahelical protein design for diverse oxidoreductase functions.
Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 73 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
73 citing papers in PubMed, 143 citations in OpenAlex.
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- Small-molecule binding and sensing with a designed protein family.Nature communications · 2026Article
- Unraveling Charge-Transfer States and Their Ultrafast Dynamics in Artificial Light-Harvesting Complexes.ACS physical chemistry Au · 2026Article
- De novo design of four-helix bundle proteins to bind metalloporphyrin cofactors.Methods in enzymology · 2025Article
- Mn-porphyrins in a four-helix bundle participate in photo-induced electron transfer with a bacterial reaction center.Photosynthesis research · 2024Article
- Spiers Memorial Lecture: Engineering biocatalysts.Faraday discussions · 2024Article
- Computational design of de novo bioenergetic membrane proteins.Biochemical Society transactions · 2024Review
- Delineating redox cooperativity in water-soluble and membrane multiheme cytochromes through protein design.Protein science : a publication of the Protein Society · 2024Article
- Controlling heme redox properties in peptide amphiphile fibers with sequence and heme loading ratio.Biophysical journal · 2024Article
- De novo design of proteins housing excitonically coupled chlorophyll special pairs.Nature chemical biology · 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
- Design of Heme Enzymes with a Tunable Substrate Binding Pocket Adjacent to an Open Metal Coordination Site.Journal of the American Chemical Society · 2023Article
- Article
- Cellular production of a de novo membrane cytochrome.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Engineering excitonically coupled dimers in an artificial protein for light harvesting via computational modeling.Protein science : a publication of the Protein Society · 2023Article
- Tailorable Tetrahelical Bundles as a Toolkit for Redox Studies.The journal of physical chemistry. B · 2022Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- De novo protein design of photochemical reaction centers.Nature communications · 2022Article
13 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
- Erratum issued
Authors and funding
17 authors at 2 institutions in 3 countries.
Funding
Abstract
Emulating functions of natural enzymes in man-made constructs has proven challenging. Here we describe a man-made protein platform that reproduces many of the diverse functions of natural oxidoreductases without importing the complex and obscure interactions common to natural proteins. Our design is founded on an elementary, structurally stable 4-α-helix protein monomer with a minimalist interior malleable enough to accommodate various light- and redox-active cofactors and with an exterior tolerating extensive charge patterning for modulation of redox cofactor potentials and environmental interactions. Despite its modest size, the construct offers several independent domains for functional engineering that targets diverse natural activities, including dioxygen binding and superoxide and peroxide generation, interprotein electron transfer to natural cytochrome c and light-activated intraprotein energy transfer and charge separation approximating the core reactions of photosynthesis, cryptochrome and photolyase. The highly stable, readily expressible and biocompatible characteristics of these open-ended designs promise development of practical in vitro and in vivo applications.
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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.