ArticleMethods in enzymology2016
De Novo Construction of Redox Active Proteins.
Article in Methods in enzymology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Selection for growth drives the emergence of genetic heredity in protocells.PLoS biology · 2026Article
- Article
- Engineering excitonically coupled dimers in an artificial protein for light harvesting via computational modeling.Protein science : a publication of the Protein Society · 2023Article
- De novo protein design of photochemical reaction centers.Nature communications · 2022Article
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- Rational design of photosynthetic reaction center protein maquettes.Frontiers in molecular biosciences · 2022Article
- The pH-Induced Selectivity Between Cysteine or Histidine Coordinated Heme in an Artificial α-Helical Metalloprotein.Angewandte Chemie (International ed. in English) · 2021Article
- Ultrafast flavin/tryptophan radical pair kinetics in a magnetically sensitive artificial protein.Physical chemistry chemical physics : PCCP · 2019Article
- Designed for life: biocompatible de novo designed proteins and components.Journal of the Royal Society, Interface · 2018Review
- An Artificial Heme Enzyme for Cyclopropanation Reactions.Angewandte Chemie (International ed. in English) · 2018Article
- De novo synthetic biliprotein design, assembly and excitation energy transfer.Journal of the Royal Society, Interface · 2018Article
- Multi-step excitation energy transfer engineered in genetic fusions of natural and synthetic light-harvesting proteins.Journal of the Royal Society, Interface · 2017Article
- Engineering an Artificial Flavoprotein Magnetosensor.Journal of the American Chemical Society · 2016Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Relatively simple principles can be used to plan and construct de novo proteins that bind redox cofactors and participate in a range of electron-transfer reactions analogous to those seen in natural oxidoreductase proteins. These designed redox proteins are called maquettes. Hydrophobic/hydrophilic binary patterning of heptad repeats of amino acids linked together in a single-chain self-assemble into 4-alpha-helix bundles. These bundles form a robust and adaptable frame for uncovering the default properties of protein embedded cofactors independent of the complexities introduced by generations of natural selection and allow us to better understand what factors can be exploited by man or nature to manipulate the physical chemical properties of these cofactors. Anchoring of redox cofactors such as hemes, light active tetrapyrroles, FeS clusters, and flavins by His and Cys residues allow cofactors to be placed at positions in which electron-tunneling rates between cofactors within or between proteins can be predicted in advance. The modularity of heptad repeat designs facilitates the construction of electron-transfer chains and novel combinations of redox cofactors and new redox cofactor assisted functions. Developing de novo designs that can support cofactor incorporation upon expression in a cell is needed to support a synthetic biology advance that integrates with natural bioenergetic pathways.
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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.