ReviewBiochemical Society transactions2012
Engineering oxidoreductases: maquette proteins designed from scratch.
Review in Biochemical Society transactions, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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.
The trial behind it
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
25 citing papers in PubMed, 60 citations in OpenAlex.
- De novo design of porphyrin-containing proteins as efficient and stereoselective catalysts.Science (New York, N.Y.) · 2025Article
- 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
- 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
- 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
- Comprehensive strategies of machine-learning-based quantitative structure-activity relationship models.iScience · 2021Review
- Hydrogen bonding rearrangement by a mitochondrial disease mutation in cytochromeProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Recent Progress Using De Novo Design to Study Protein Structure, Design and Binding Interactions.Life (Basel, Switzerland) · 2021Review
- Review
- An efficient, step-economical strategy for the design of functional metalloproteins.Nature chemistry · 2019Article
- Thawing out frozen metabolic accidents.BMC biology · 2019Review
- The ascent of man(made oxidoreductases).Current opinion in structural biology · 2018Review
- Designed for life: biocompatible de novo designed proteins and components.Journal of the Royal Society, Interface · 2018Review
- A synthetic biological quantum optical system.Nanoscale · 2018Article
- Probing the quality control mechanism of theThe Journal of biological chemistry · 2018Article
- De novo synthetic biliprotein design, assembly and excitation energy transfer.Journal of the Royal Society, Interface · 2018Article
- Design and engineering of artificial oxygen-activating metalloenzymes.Chemical Society reviews · 2016Review
Corrections and comments
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Authors and funding
19 authors at 4 institutions in 2 countries.
Funding
Abstract
The study of natural enzymes is complicated by the fact that only the most recent evolutionary progression can be observed. In particular, natural oxidoreductases stand out as profoundly complex proteins in which the molecular roots of function, structure and biological integration are collectively intertwined and individually obscured. In the present paper, we describe our experimental approach that removes many of these often bewildering complexities to identify in simple terms the necessary and sufficient requirements for oxidoreductase function. Ours is a synthetic biology approach that focuses on from-scratch construction of protein maquettes designed principally to promote or suppress biologically relevant oxidations and reductions. The approach avoids mimicry and divorces the commonly made and almost certainly false ascription of atomistically detailed functionally unique roles to a particular protein primary sequence, to gain a new freedom to explore protein-based enzyme function. Maquette design and construction methods make use of iterative steps, retraceable when necessary, to successfully develop a protein family of sturdy and versatile single-chain three- and four-α-helical structural platforms readily expressible in bacteria. Internally, they prove malleable enough to incorporate in prescribed positions most natural redox cofactors and many more simplified synthetic analogues. External polarity, charge-patterning and chemical linkers direct maquettes to functional assembly in membranes, on nanostructured titania, and to organize on selected planar surfaces and materials. These protein maquettes engage in light harvesting and energy transfer, in photochemical charge separation and electron transfer, in stable dioxygen binding and in simple oxidative chemistry that is the basis of multi-electron oxidative and reductive catalysis.
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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.