ArticleJournal of the American Chemical Society2012
Azurin as a protein scaffold for a low-coordinate nonheme iron site with a small-molecule binding pocket.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Exploring the Role of Azurin from the Endophytic BacteriumMicroorganisms · 2026Article
- Azurin: A Model to Study a Metal Coordination Sphere or Electron Transfer in Metalloproteins.International journal of molecular sciences · 2025Review
- Iron Insertion at the Assembly Site of the ISCU Scaffold Protein Is a Conserved Process Initiating Fe-S Cluster Biosynthesis.Journal of the American Chemical Society · 2022Article
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Repurposing metalloproteins as mimics of natural metalloenzymes for small-molecule activation.Journal of inorganic biochemistry · 2021Review
- 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
- Artificial Iron Proteins: Modeling the Active Sites in Non-Heme Dioxygenases.Inorganic chemistry · 2020Article
- Physiologically relevant reconstitution of iron-sulfur cluster biosynthesis uncovers persulfide-processing functions of ferredoxin-2 and frataxin.Nature communications · 2019Article
- An efficient, step-economical strategy for the design of functional metalloproteins.Nature chemistry · 2019Article
- Understanding and Modulating Metalloenzymes with Unnatural Amino Acids, Non-Native Metal Ions, and Non-Native Metallocofactors.Accounts of chemical research · 2019Article
- The Periodic Table's Impact on Bioinorganic Chemistry and Biology's Selective Use of Metal Ions.Structure and bonding · 2019Article
- Supramolecular Porphyrin Cages Assembled at Molecular-Materials Interfaces for Electrocatalytic CO Reduction.ACS central science · 2017Article
- Density Functional Calculations for Prediction ofACS omega · 2017Article
- An internal electron reservoir enhances catalytic CO2 reduction by a semisynthetic enzyme.Chemical communications (Cambridge, England) · 2016Article
- Enzyme Substrate Complex of the H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Mössbauer and Computational Studies.Inorganic chemistry · 2016Article
- A single protein redox ruler.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Generation of high-spin iron(I) in a protein environment using cryoreduction.Inorganic chemistry · 2013Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
The apoprotein of Pseudomonas aeruginosa azurin binds iron(II) to give a 1:1 complex, which has been characterized by electronic absorption, Mössbauer, and NMR spectroscopies, as well as X-ray crystallography and quantum-chemical computations. Despite potential competition by water and other coordinating residues, iron(II) binds tightly to the low-coordinate site. The iron(II) complex does not react with chemical redox agents to undergo oxidation or reduction. Spectroscopically calibrated quantum-chemical computations show that the complex has high-spin iron(II) in a pseudotetrahedral coordination environment, which features interactions with side chains of two histidines and a cysteine as well as the C═O of Gly45. In the (5)A(1) ground state, the d(z(2)) orbital is doubly occupied. Mutation of Met121 to Ala leaves the metal site in a similar environment but creates a pocket for reversible binding of small anions to the iron(II) center. Specifically, azide forms a high-spin iron(II) complex and cyanide forms a low-spin iron(II) complex.
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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.