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Why copper is preferred over iron for oxygen activation and reduction in haem-copper oxidases
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/ange.201308431openalex-snapshot
Spectroscopic and Computational Study of a Nonheme Iron Nitrosyl Center in a Biosynthetic Model of Nitric Oxide Reductase
inferredcites →https://doi.org/10.1002/anie.201108756openalex-snapshot
Significant Increase of Oxidase Activity through the Genetic Incorporation of a Tyrosine–Histidine Cross‐Link in a Myoglobin Model of Heme–Copper Oxidase
inferredcites →https://doi.org/10.1002/anie.201201981openalex-snapshot
A Designed Functional Metalloenzyme that Reduces O 2 to H 2 O with Over One Thousand Turnovers
inferredcites →https://doi.org/10.1002/anie.201308431openalex-snapshot
Spectroscopic and Computational Study of a Nonheme Iron Nitrosyl Center in a Biosynthetic Model of Nitric Oxide Reductase
inferredcites →https://doi.org/10.1002/hc.10094openalex-snapshot
Designer haem proteins: What can we learn from protein engineering?
inferredcites →https://doi.org/10.1007/1-4020-4254-x_34openalex-snapshot
De Novo Protein Design in Respiration and Photosynthesis
inferredcites →https://doi.org/10.1007/s10863-008-9181-7openalex-snapshot
Cytochrome c oxidase: exciting progress and remaining mysteries
inferredcites →https://doi.org/10.1016/0005-2728(92)90222-nopenalex-snapshot
O2 activation in cytochrome oxidase and in other heme proteins
inferredcites →https://doi.org/10.1016/0014-5793(94)80228-9openalex-snapshot
Cytochrome oxidase evolved by tinkering with denitrification enzymes
inferredcites →https://doi.org/10.1016/j.bbabio.2003.07.013openalex-snapshot
Cytochrome c oxidase: 25 years of the elusive proton pump
inferredcites →https://doi.org/10.1016/j.bbabio.2011.09.020openalex-snapshot
The superfamily of heme–copper oxygen reductases: Types and evolutionary considerations
inferredcites →https://doi.org/10.1016/j.ccr.2012.05.008openalex-snapshot
CO, NO and O2 as vibrational probes of heme protein interactions
inferredcites →https://doi.org/10.1016/j.ccr.2013.02.007openalex-snapshot
Designing functional metalloproteins: From structural to catalytic metal sites
inferredcites →https://doi.org/10.1016/j.febslet.2004.04.027openalex-snapshot
Structural elements involved in electron-coupled proton transfer in cytochrome c oxidase
inferredcites →https://doi.org/10.1016/j.febslet.2011.08.037openalex-snapshot
Cytochromecoxidase: Intermediates of the catalytic cycle and their energy‐coupled interconversion
inferredcites →https://doi.org/10.1016/j.jinorgbio.2004.09.024openalex-snapshot
Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme?copper oxidase type
inferredcites →https://doi.org/10.1016/s0021-9258(18)53138-0openalex-snapshot
The mechanism of autooxidation of myoglobin.
inferredcites →https://doi.org/10.1016/s0898-8838(00)51000-9openalex-snapshot
Chemical reactivity of the active site of myoglobin
inferredcites →https://doi.org/10.1016/s0968-0004(00)89098-2openalex-snapshot
Evolution of energetic metabolism: the respiration-early hypothesis
inferredcites →https://doi.org/10.1021/acs.accounts.5b00265openalex-snapshot
Synthetic Heme/Copper Assemblies: Toward an Understanding of Cytochrome c Oxidase Interactions with Dioxygen and Nitrogen Oxides
inferredcites →https://doi.org/10.1021/acs.chemrev.8b00074openalex-snapshot
Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function
inferredcites →https://doi.org/10.1021/acs.inorgchem.5b01105openalex-snapshot
Recent Advances in Biosynthetic Modeling of Nitric Oxide Reductases and Insights Gained from Nuclear Resonance Vibrational and Other Spectroscopic Studies
inferredcites →https://doi.org/10.1021/bi00349a023openalex-snapshot
Spectroelectrochemical study of the cytochrome a site in carbon monoxide-inhibited cytochrome c oxidase
inferredcites →https://doi.org/10.1021/bi050524hopenalex-snapshot
Electron/Proton Coupling in Bacterial Nitric Oxide Reductase during Reduction of Oxygen
inferredcites →https://doi.org/10.1021/cr0206162openalex-snapshot
Synthetic Models for Heme−Copper Oxidases
inferredcites →https://doi.org/10.1021/cr1002003openalex-snapshot
Proton-Coupled Electron Transfer in Cytochrome Oxidase
inferredcites →https://doi.org/10.1021/cr400458xopenalex-snapshot
Protein Design: Toward Functional Metalloenzymes
inferredcites →https://doi.org/10.1021/ic100472popenalex-snapshot
Recent Applications of a Synthetic Model of Cytochrome c Oxidase: Beyond Functional Modeling†This award article is an extended version of the Ronald Breslow Award for Achievement in Biomimetic Chemistry, 2009, presented at the 237th American Chemical Society National Meeting at Salt Lake City, UT.
inferredcites →https://doi.org/10.1021/ic500363hopenalex-snapshot
Linking Chemical Electron–Proton Transfer to Proton Pumping in Cytochrome c Oxidase: Broken-Symmetry DFT Exploration of Intermediates along the Catalytic Reaction Pathway of the Iron–Copper Dinuclear Complex
inferredcites →https://doi.org/10.1021/ja036949dopenalex-snapshot
Resonance Raman Spectroscopic Studies of Hydroperoxo-Myoglobin at Cryogenic Temperatures
inferredcites →https://doi.org/10.1021/ja0401242openalex-snapshot
On the Mössbauer Spectra of Isopenicillin N Synthase and a Model {FeNO}7 (S = 3/2) System
inferredcites →https://doi.org/10.1021/ja067209iopenalex-snapshot
Distinct Reaction Pathways Followed upon Reduction of Oxy-Heme Oxygenase and Oxy-Myoglobin as Characterized by Mössbauer Spectroscopy
inferredcites →https://doi.org/10.1021/ja075978bopenalex-snapshot
NMR Hyperfine Shifts in Blue Copper Proteins: A Quantum Chemical Investigation
inferredcites →https://doi.org/10.1021/ja076108xopenalex-snapshot
Structural Characterization of the Fleeting Ferric Peroxo Species in Myoglobin: Experiment and Theory
inferredcites →https://doi.org/10.1021/ja204072jopenalex-snapshot
HNO Binding in a Heme Protein: Structures, Spectroscopic Properties, and Stabilities
inferredcites →https://doi.org/10.1021/ja4091885openalex-snapshot
Direct EPR Observation of a Tyrosyl Radical in a Functional Oxidase Model in Myoglobin during both H 2 O 2 and O 2 Reactions
inferredcites →https://doi.org/10.1021/ja5054863openalex-snapshot
Systematic Tuning of Heme Redox Potentials and Its Effects on O2 Reduction Rates in a Designed Oxidase in Myoglobin
inferredcites →https://doi.org/10.1021/ja5109936openalex-snapshot
Defining the Role of Tyrosine and Rational Tuning of Oxidase Activity by Genetic Incorporation of Unnatural Tyrosine Analogs
inferredcites →https://doi.org/10.1021/ja805434mopenalex-snapshot
Nature of the Fe−O2Bonding in Oxy-Myoglobin: Effect of the Protein
inferredcites →https://doi.org/10.1021/ja9006723openalex-snapshot
Mössbauer, NMR, Geometric, and Electronic Properties in S = 3/2 Iron Porphyrins
inferredcites →https://doi.org/10.1021/ja991195hopenalex-snapshot
Design and Creation of a Cu(II)-Binding Site in Cytochrome c Peroxidase that Mimics the CuB-heme Center in Terminal Oxidases
inferredcites →https://doi.org/10.1021/jacs.5b07119openalex-snapshot
A Designed Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme
inferredcites →https://doi.org/10.1038/nature08551openalex-snapshot
Rationally tuning the reduction potential of a single cupredoxin beyond the natural range
inferredcites →https://doi.org/10.1038/nature08620openalex-snapshot
Rational Design of a Structural and Functional Nitric Oxide Reductase
inferredcites →https://doi.org/10.1038/nchem.1894openalex-snapshot
Short peptides self-assemble to produce catalytic amyloids
inferredcites →https://doi.org/10.1038/ncomms9467openalex-snapshot
A biosynthetic model of cytochrome c oxidase as an electrocatalyst for oxygen reduction
inferredcites →https://doi.org/10.1042/bj2740723openalex-snapshot
Redox analysis of the cytochrome o-type quinol oxidase complex of Escherichia coli reveals three redox components
inferredcites →https://doi.org/10.1073/pnas.0904634106openalex-snapshot
O 2 reduction by a functional heme/nonheme bis-iron NOR model complex
inferredcites →https://doi.org/10.1073/pnas.1000526107openalex-snapshot
Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin
inferredcites →https://doi.org/10.1073/pnas.1018191108openalex-snapshot
Design of a switchable eliminase
inferredcites →https://doi.org/10.1073/pnas.96.23.12971openalex-snapshot
How oxygen is activated and reduced in respiration
inferredcites →https://doi.org/10.1128/jb.183.1.189-199.2001openalex-snapshot
Two Conserved Glutamates in the Bacterial Nitric Oxide Reductase Are Essential for Activity but Not Assembly of the Enzyme
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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inferred← citeshttps://doi.org/10.1021/acs.chemrev.7b00180openalex-snapshot
Biomimetic Reactivity of Oxygen-Derived Manganese and Iron Porphyrinoid Complexes
inferred← citeshttps://doi.org/10.1021/acs.chemrev.7b00373openalex-snapshot
Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins
inferred← citeshttps://doi.org/10.1021/acs.chemrev.7b00664openalex-snapshot
Oxygen Activation and Energy Conservation by Cytochrome c Oxidase
inferred← citeshttps://doi.org/10.1021/acs.chemrev.8b00074openalex-snapshot
Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function
inferred← citeshttps://doi.org/10.1021/acs.inorgchem.2c01898openalex-snapshot
Symmetry-Adapted Synthesis of Dicopper Oxidases with Divergent Dioxygen Reactivity
inferred← citeshttps://doi.org/10.1021/acs.inorgchem.4c03093openalex-snapshot
Rational Design of an Artificial Metalloenzyme by Constructing a Metal-Binding Site Close to the Heme Cofactor in Myoglobin
inferred← citeshttps://doi.org/10.1021/acs.jchemed.2c00533openalex-snapshot
Introducing the Role of Metals in Biology to High School Students
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.9b01069openalex-snapshot
Porphyrinoid–Cyclodextrin Assemblies in Biomedical Research: An Update
inferred← citeshttps://doi.org/10.1021/acs.jpca.4c03777openalex-snapshot
A Common Bottleneck for Metal Oxidation by Molecular Oxygen Across Size Regimes: Kinetics of Atomic Lanthanide Cations (La+–Lu+) with O2
inferred← citeshttps://doi.org/10.1021/acs.jpca.9b05185openalex-snapshot
Catalytic CO Oxidation by Gas-Phase Metal Oxide Clusters
inferred← citeshttps://doi.org/10.1021/acsaem.1c01753openalex-snapshot
Four-Electron Electrocatalytic O2 Reduction by a Ferrocene-Modified Glutathione Complex of Cu
inferred← citeshttps://doi.org/10.1021/acsami.7b02022openalex-snapshot
Mild and Selective C–H Activation of COC Microfluidic Channels Allowing Covalent Multifunctional Coatings
inferred← citeshttps://doi.org/10.1021/acsami.8b02367openalex-snapshot
Molecular O2 Activation over Cu(I)-Mediated C≡N Bond for Low-Temperature CO Oxidation
inferred← citeshttps://doi.org/10.1021/acsami.8b10594openalex-snapshot
Preparation and Characterization of Chiral Transition-Metal Dichalcogenide Quantum Dots and Their Enantioselective Catalysis
inferred← citeshttps://doi.org/10.1021/acscatal.0c04753openalex-snapshot
Impact of Heterometallic Cooperativity of Iron and Copper Active Sites on Electrocatalytic Oxygen Reduction Kinetics
inferred← citeshttps://doi.org/10.1021/acscatal.5c05262openalex-snapshot
Deciphering the Coordination Environment’s Impact on O–O Activation in Dicopper Enzymes: Computational Insights from AhyBURP Peptide Cyclase
inferred← citeshttps://doi.org/10.1021/acscatal.8b02240openalex-snapshot
O2 Reduction by Biosynthetic Models of Cytochrome c Oxidase: Insights into Role of Proton Transfer Residues from Perturbed Active Sites Models of CcO
inferred← citeshttps://doi.org/10.1021/acsenergylett.2c01132openalex-snapshot
Oxygen-Plasma-Treated Fe–N–C Catalysts with Dual Binding Sites for Enhanced Electrocatalytic Polysulfide Conversion in Lithium–Sulfur Batteries
inferred← citeshttps://doi.org/10.1021/acsenergylett.9b01308openalex-snapshot
Engineered Enzymes and Bioinspired Catalysts for Energy Conversion
inferred← citeshttps://doi.org/10.1021/acsnano.2c12799openalex-snapshot
In Situ Microscopic Studies on the Interaction of Multi-Principal Element Nanoparticles and Bacteria
inferred← citeshttps://doi.org/10.1021/acsnano.7b03195openalex-snapshot
Self-Assembled DNA/Peptide-Based Nanoparticle Exhibiting Synergistic Enzymatic Activity
inferred← citeshttps://doi.org/10.1021/acsomega.5c07728openalex-snapshot
Oxidative HNO Formation Mechanisms from NH 2 OH via Two Different Heme Proteins and Effects from Hemes, Nearby Residues, and Protein Environments
inferred← citeshttps://doi.org/10.1021/jacs.0c10135openalex-snapshot
Ligand Field Inversion as a Mechanism to Gate Bioorganometallic Reactivity: Investigating a Biochemical Model of Acetyl CoA Synthase Using Spectroscopy and Computation
inferred← citeshttps://doi.org/10.1021/jacs.1c03510openalex-snapshot
Defect Engineering Enables Synergistic Action of Enzyme-Mimicking Active Centers for High-Efficiency Tumor Therapy
inferred← citeshttps://doi.org/10.1021/jacs.2c09608openalex-snapshot
“Electron Transport Chain Interference” Strategy of Amplified Mild-Photothermal Therapy and Defect-Engineered Multi-Enzymatic Activities for Synergistic Tumor-Personalized Suppression
inferred← citeshttps://doi.org/10.1021/jacs.2c10988openalex-snapshot
Mechanical Interlocking Enhances the Electrocatalytic Oxygen Reduction Activity and Selectivity of Molecular Copper Complexes
inferred← citeshttps://doi.org/10.1021/jacs.6c00223openalex-snapshot
Direct Comparison of CuB and CuSiR Sites in a Single Designed Protein Scaffold Reveals a Central Role for Tyrosine in Oxygen and Sulfite Reduction
inferred← citeshttps://doi.org/10.1021/jacs.7b05800openalex-snapshot
Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism
inferred← citeshttps://doi.org/10.1021/jacsau.5c00438openalex-snapshot
Oxidative and Hydrolytic HNO Formation from a Clinical Drug Hydroxyurea Catalyzed by Horseradish Peroxidase: Basic Mechanism, Active Site Effect, and Implications for Drug Design
inferred← citeshttps://doi.org/10.1038/s41586-022-04456-zopenalex-snapshot
The road to fully programmable protein catalysis
inferred← citeshttps://doi.org/10.1038/s41929-020-00563-0openalex-snapshot
Simultaneous oxidative and reductive reactions in one system by atomic design
inferred← citeshttps://doi.org/10.1039/9781788012911-00037openalex-snapshot
Design and Engineering of Heme Enzymes With O2-dependent Catalytic Activity
inferred← citeshttps://doi.org/10.1039/c6qi00603eopenalex-snapshot
Understanding the choice of copper by heme-copper oxidase using biosynthetic models in myoglobin
inferred← citeshttps://doi.org/10.1039/c7ra09285gopenalex-snapshot
Redox-active copper triangles as an enzymatic molecular flask for light-driven hydrogen production
inferred← citeshttps://doi.org/10.1039/c7sc04732kopenalex-snapshot
A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome c oxidase
inferred← citeshttps://doi.org/10.1039/c9se00229dopenalex-snapshot
Chicken fat for catalysis: a scaffold is as important for molecular complexes for energy transformations as it is for enzymes in catalytic function
inferred← citeshttps://doi.org/10.1039/c9ta03518dopenalex-snapshot
A copper single-atom catalyst towards efficient and durable oxygen reduction for fuel cells
inferred← citeshttps://doi.org/10.1039/d0cc03137bopenalex-snapshot
Proteins as diverse, efficient, and evolvable scaffolds for artificial metalloenzymes
inferred← citeshttps://doi.org/10.1039/d0cs01297aopenalex-snapshot
Molecular understanding of heteronuclear active sites in heme–copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling
inferred← citeshttps://doi.org/10.1039/d0cs01456gopenalex-snapshot
Transition metal-mediated O–O bond formation and activation in chemistry and biology
inferred← citeshttps://doi.org/10.1039/d1se01635kopenalex-snapshot
Strong metal–support interaction in copper hexacyanoferrate nanocube decorated functionalized multiwall carbon nanotubes for enhanced bi-functional oxygen electrocatalytic activity and stability
inferred← citeshttps://doi.org/10.1039/d1ta09459aopenalex-snapshot
Cu II /Cu I decorated N-doped carbonaceous electrocatalysts for the oxygen reduction reaction
inferred← citeshttps://doi.org/10.1039/d2ey00055eopenalex-snapshot
Fe–N/C catalysts with tunable mesoporous structures and carbon layer numbers reveal the role of interlayer O 2 activation
inferred← citeshttps://doi.org/10.1039/d3ob01687kopenalex-snapshot
Application of engineered myoglobins for biosynthesis of clofazimine by integration with chemical synthesis
inferred← citeshttps://doi.org/10.1039/d5ta00879dopenalex-snapshot
Synergistic construction of defect-rich nanozymes via montmorillonite support loading and iron doping for enhanced peroxidase-like activity
inferred← citeshttps://doi.org/10.1039/d6cc04693bopenalex-snapshot
Cu–N active site enriched Cu–ATz complex with potential-induced dynamic coordination evolution for oxygen reduction reaction
inferred← citeshttps://doi.org/10.1042/ebc20230012openalex-snapshot
Oxidoreductases and metal cofactors in the functioning of the earth
inferred← citeshttps://doi.org/10.1063/5.0271813openalex-snapshot
Electronic structure regulation via heterojunction engineering for enhanced oxygen reduction reaction
inferred← citeshttps://doi.org/10.1073/pnas.1720298115openalex-snapshot
Heme redox potentials hold the key to reactivity differences between nitric oxide reductase and heme-copper oxidase
inferred← citeshttps://doi.org/10.1073/pnas.2123022119openalex-snapshot
Thioester synthesis by a designed nickel enzyme models prebiotic energy conversion
inferred← citeshttps://doi.org/10.1080/01614940.2021.1919044openalex-snapshot
Low-Temperature Heterogeneous Oxidation Catalysis and Molecular Oxygen Activation
inferred← citeshttps://doi.org/10.1088/2632-959x/abe455openalex-snapshot
Nano-mediated uniform ternary Cu–Co–Ni-based nitrogen-doped carbon nanotubes with synergistic reactivity for high-performance oxygen reduction
inferred← citeshttps://doi.org/10.1093/bulcsj/uoag071openalex-snapshot
Computational investigation of FeCuN co-doped graphene as a bimetallic electrocatalyst for oxygen reduction reaction
inferred← citeshttps://doi.org/10.1101/2025.05.27.656425openalex-snapshot
Rational design of tertiary coordination sphere of a heme-based sensor for two-orders enhanced oxygen affinity
inferred← citeshttps://doi.org/10.1101/426874openalex-snapshot
The Structure of Oxalate Decarboxylase at its Active pH
inferred← citeshttps://doi.org/10.1126/sciadv.ady3842openalex-snapshot
Remolding laccase for whole-cell and in vivo modulation of dopamine signal
inferred← citeshttps://doi.org/10.1142/s1088424623500748openalex-snapshot
A cobalt corrole with a biologically relevant imidazolium pendant for boosted electrocatalytic oxygen reduction
inferred← citeshttps://doi.org/10.1155/2020/8516105openalex-snapshot
Consumption of Raw Herbal Medicines Is Associated with Major Public Health Risks amongst Ugandans
inferred← citeshttps://doi.org/10.1380/ejssnt.2020.81openalex-snapshot
Electrocatalytic Oxygen Reduction at Multinuclear Metal Active Sites Inspired by Metalloenzymes
inferred← citeshttps://doi.org/10.31223/x58h36openalex-snapshot
Oxidoreductases and metal cofactors in the functioning of Earth
inferred← citeshttps://doi.org/10.3389/fmicb.2019.00499openalex-snapshot
Oxygen Reductases in Alphaproteobacterial Genomes: Physiological Evolution From Low to High Oxygen Environments
inferred← citeshttps://doi.org/10.3389/fnut.2021.592340openalex-snapshot
Descriptive Analysis of Heavy Metals Content of Beef From Eastern Uganda and Their Safety for Public Consumption
inferred← citeshttps://doi.org/10.3390/biomedicines9040391openalex-snapshot
ATP7A-Regulated Enzyme Metalation and Trafficking in the Menkes Disease Puzzle
inferred← citeshttps://doi.org/10.3390/microorganisms9102044openalex-snapshot
Learning from Yeast about Mitochondrial Carriers
inferred← citeshttps://doi.org/10.3390/molecules24152743openalex-snapshot
Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters
inferred← citeshttps://doi.org/10.3390/molecules27238478openalex-snapshot
O2 Carrier Myoglobin Also Exhibits β-Lactamase Activity That Is Regulated by the Heme Coordination State
inferred← citeshttps://doi.org/10.5483/bmbrep.2023-0172openalex-snapshot
Coordination chemistry of mitochondrial copper metalloenzymes: exploring implications for copper dyshomeostasis in cell death
inferred← citeshttps://doi.org/10.70675/9874c0a7z154az49c8za875zde5f1b73d5adopenalex-snapshot
Complexification d'un système LCu(I) pour la coordination et l'activation du dioxygène : étude par spectrométrie de masse et DFT
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