ArticleNature communications2015
A biosynthetic model of cytochrome c oxidase as an electrocatalyst for oxygen reduction.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 114 citations in OpenAlex.
- Enzymatic oxygen reduction dominates overpotential-driven thermogenesis in mitochondria.Chemical science · 2026Article
- 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
- Molecular architectures of iron complexes for oxygen reduction catalysis-Activity enhancement by hydroxide ions coupling.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Review
- Engineering an Oxygen-Binding Protein for Photocatalytic COAngewandte Chemie (International ed. in English) · 2023Article
- Bioinspired and Bioderived Aqueous Electrocatalysis.Chemical reviews · 2023Review
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Review
- HCoordination chemistry reviews · 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
- The Periodic Table's Impact on Bioinorganic Chemistry and Biology's Selective Use of Metal Ions.Structure and bonding · 2019Article
- Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.Chemical reviews · 2018Review
- OACS catalysis · 2018Article
- Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.Chemical reviews · 2018Review
- Insights Into How Heme Reduction Potentials Modulate Enzymatic Activities of a Myoglobin-based Functional Oxidase.Angewandte Chemie (International ed. in English) · 2017Article
- Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities.Israel journal of chemistry · 2016Article
- Design and engineering of artificial oxygen-activating metalloenzymes.Chemical Society reviews · 2016Review
- Polydopamine-Coated Manganese Complex/Graphene Nanocomposite for Enhanced Electrocatalytic Activity Towards Oxygen Reduction.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Creating an artificial functional mimic of the mitochondrial enzyme cytochrome c oxidase (CcO) has been a long-term goal of the scientific community as such a mimic will not only add to our fundamental understanding of how CcO works but may also pave the way for efficient electrocatalysts for oxygen reduction in hydrogen/oxygen fuel cells. Here we develop an electrocatalyst for reducing oxygen to water under ambient conditions. We use site-directed mutants of myoglobin, where both the distal Cu and the redox-active tyrosine residue present in CcO are modelled. In situ Raman spectroscopy shows that this catalyst features very fast electron transfer rates, facile oxygen binding and O-O bond lysis. An electron transfer shunt from the electrode circumvents the slow dissociation of a ferric hydroxide species, which slows down native CcO (bovine 500 s(-1)), allowing electrocatalytic oxygen reduction rates of 5,000 s(-1) for these biosynthetic models.
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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.