ArticleJournal of the American Chemical Society2015
A Designed Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 86 citations in OpenAlex.
- A Minimalist Iron Porphyrin Which Can Catalyze Both Peroxidation and Oxygen Reduction Reaction.JACS Au · 2025Article
- A Post-translational Histidine-Histidine Cross-Link Enhances Enzymatic Oxygen Reduction Activity with Greater pH Adaptability.Journal of the American Chemical Society · 2025Article
- Study and design of amino acid-based radical enzymes using unnatural amino acids.RSC chemical biology · 2023Article
- Engineering an Oxygen-Binding Protein for Photocatalytic COAngewandte Chemie (International ed. in English) · 2023Article
- Mechanistic and structural characterization of an iridium-containing cytochrome reveals kinetically relevant cofactor dynamics.Nature catalysis · 2023Article
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Thioester synthesis by a designed nickel enzyme models prebiotic energy conversion.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Designer Heme Proteins: Achieving Novel Function with Abiological Heme Analogues.Accounts of chemical research · 2021Article
- Review
- Identifying metal binding amino acids based on backbone geometries as a tool for metalloprotein engineering.Protein science : a publication of the Protein Society · 2021Article
- Abiological catalysis by myoglobin mutant with a genetically incorporated unnatural amino acid.The Biochemical journal · 2021Article
- De novo biosynthesis of a nonnatural cobalt porphyrin cofactor inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.Chemical Society reviews · 2021Review
- An Engineered Glutamate in Biosynthetic Models of Heme-Copper Oxidases Drives Complete Product Selectivity by Tuning the Hydrogen-Bonding Network.Biochemistry · 2021Article
- Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters.Molecules (Basel, Switzerland) · 2019Review
- Formation and Reactivity of New Isoporphyrins: Implications for Understanding the Tyr-His Cross-Link Cofactor Biogenesis in CytochromeJournal of the American Chemical Society · 2019Article
- Understanding and Modulating Metalloenzymes with Unnatural Amino Acids, Non-Native Metal Ions, and Non-Native Metallocofactors.Accounts of chemical research · 2019Article
- Artificial Heme Enzymes for the Construction of Gold-Based Biomaterials.International journal of molecular sciences · 2018Article
- A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme.Science (New York, N.Y.) · 2018Article
- ICBS 2017 in Shanghai-Illuminating Life with Chemical Innovation.ACS chemical biology · 2018Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
Terminal oxidases catalyze four-electron reduction of oxygen to water, and the energy harvested is utilized to drive the synthesis of adenosine triphosphate. While much effort has been made to design a catalyst mimicking the function of terminal oxidases, most biomimetic catalysts have much lower activity than native oxidases. Herein we report a designed oxidase in myoglobin with an O2 reduction rate (52 s(-1)) comparable to that of a native cytochrome (cyt) cbb3 oxidase (50 s(-1)) under identical conditions. We achieved this goal by engineering more favorable electrostatic interactions between a functional oxidase model designed in sperm whale myoglobin and its native redox partner, cyt b5, resulting in a 400-fold electron transfer (ET) rate enhancement. Achieving high activity equivalent to that of native enzymes in a designed metalloenzyme offers deeper insight into the roles of tunable processes such as ET in oxidase activity and enzymatic function and may extend into applications such as more efficient oxygen reduction reaction catalysts for biofuel cells.
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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.