ArticleNature chemistry2009
Type-zero copper proteins.
Article in Nature chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 101 citations in OpenAlex.
- Protein-Enforced Ligand Environments Reshape Classical Coordination Preferences in Copper Polypyridyl Complexes.Journal of the American Chemical Society · 2026Article
- An Activity-Based Sensing Approach to Monitor Nanomaterial-Promoted Changes in Labile Metal Pools in Living Systems.Chemical & biomedical imaging · 2026Article
- When the wrong metal stops the cycle: Dynamics and specificity in plant copper-dependent peptide cyclases.Journal of inorganic biochemistry · 2026Article
- Deciphering Cu(II) EPR in biological buffers: Implications for copper protein studies.Journal of inorganic biochemistry · 2026Article
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- Controlling outer-sphere solvent reorganization energy to turn on or off the function of artificial metalloenzymes.Nature communications · 2025Article
- Crystal Lattice-Induced Stress modulates Photoinduced Jahn-Teller Distortion Dynamics.ACS physical chemistry Au · 2024Article
- Peptide Crosslinking by a Class of Plant Copper Enzymes.Trends in chemistry · 2024Article
- A designed Copper Histidine-brace enzyme for oxidative depolymerization of polysaccharides as a model of lytic polysaccharide monooxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Primary and Secondary Coordination Sphere Effects on the Structure and Function ofJournal of the American Chemical Society · 2023Article
- Electrochemical and Structural Study of the Buried Tryptophan in Azurin: Effects of Hydration and Polarity on the Redox Potential of W48.The journal of physical chemistry. B · 2023Article
- Oxidation state-specific fluorescent copper sensors reveal oncogene-driven redox changes that regulate labile copper(II) pools.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Frustration Dynamics and Electron-Transfer Reorganization Energies in Wild-Type and Mutant Azurins.Journal of the American Chemical Society · 2022Article
- Converged Structural and Spectroscopic Properties for Refined QM/MM Models of Azurin.Inorganic chemistry · 2021Article
- Stepwise nitrosylation of the nonheme iron site in an engineered azurin and a molecular basis for nitric oxide signaling mediated by nonheme iron proteins.Chemical science · 2021Article
- Trinuclear copper biocatalytic center forms an active site of thiocyanate dehydrogenase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Clarifying the Copper Coordination Environment in a de Novo Designed Red Copper Protein.Inorganic chemistry · 2018Article
- Accurate Quantum Mechanical/Molecular Mechanical Calculations of Reduction Potentials in Azurin Variants.Journal of chemical theory and computation · 2018Article
- Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis.Chemical science · 2018Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Many proteins contain copper in a range of coordination environments, where it has various biological roles, such as transferring electrons or activating dioxygen. These copper sites can be classified by their function or spectroscopic properties. Those with a single copper atom are either type 1, with an intense absorption band near 600 nm, or type 2, with weak absorption in the visible region. We have built a novel copper(II) binding site within structurally modified Pseudomonas aeruginosa azurins that does not resemble either existing type, which we therefore call 'type zero'. X-ray crystallographic analysis shows that these sites adopt distorted tetrahedral geometries, with an unusually short Cu–O (G45 carbonyl) bond. Relatively weak absorption near 800 nm and narrow parallel hyperfine splittings in electron paramagnetic resonance spectra are the spectroscopic signatures of type zero copper. Cyclic voltammetric experiments demonstrate that the electron transfer reactivities of type-zero azurins are enhanced relative to that of the corresponding type 2 (C112D) protein.
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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.