ArticleBiochemistry2015
Characterization of the Bacterioferritin/Bacterioferritin Associated Ferredoxin Protein-Protein Interaction in Solution and Determination of Binding Energy Hot Spots.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 44 citations in OpenAlex.
- Influence of heme and pH on the oligomeric states of Brucella melitensis bacterioferritin.Acta crystallographica. Section D, Structural biology · 2026Article
- Structural Analysis and Inhibitor Modeling of Bacterioferritin From Brucella abortus.Proteins · 2026Article
- Structural, functional, and evolutionary perspectives of bacterial iron repertoire: bacterioferritin and bacterioferritin-associated ferredoxin as emerging targets against antibiotic resistance.Folia microbiologica · 2026Review
- Screening of quorum Sensing-Dependent strong promoters in Pseudomonas bijieensis 2P24 for metabolic optimization and Recombinant protein production.World journal of microbiology & biotechnology · 2026Article
- The Iron-Sulfur Cluster of Bacterioferritin-Associated Ferredoxin (Bfd): a "Biological Fuse" that Prevents Oxidative Damage to Cells?Angewandte Chemie (International ed. in English) · 2025Article
- Inhibitors of the Bacterioferritin Ferredoxin Complex Dysregulate Iron Homeostasis and KillACS infectious diseases · 2025Article
- The iron metalloproteome of Pseudomonas aeruginosa under oxic and anoxic conditions.Metallomics : integrated biometal science · 2025Article
- Genome mining based on transcriptional regulatory networks uncovers a novel locus involved in desferrioxamine biosynthesis.PLoS biology · 2025Article
- A Closer Look at the FeS Heme Bonds in Azotobacter vinelandii Bacterioferritin: QM/MM and Local Mode Analysis.Journal of computational chemistry · 2025Article
- The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits.Scientific reports · 2024Article
- Draft Genome Sequence ofEvolutionary bioinformatics online · 2024Article
- Mobilization of iron stored in bacterioferritin, a new target for perturbing iron homeostasis and developing antibacterial and antibiofilm molecules.Journal of inorganic biochemistry · 2023Review
- Mechanisms of iron homeostasis in Pseudomonas aeruginosa and emerging therapeutics directed to disrupt this vital process.Microbial biotechnology · 2023Review
- Elucidation of the Correlation between Heme Distortion and Tertiary Structure of the Heme-Binding Pocket Using a Convolutional Neural Network.Biomolecules · 2022Article
- Article
- Iron Homeostasis in Pseudomonas aeruginosa: Targeting Iron Acquisition and Storage as an Antimicrobial Strategy.Advances in experimental medicine and biology · 2022Article
- Electron Transfer from Haem to the Di-Iron Ferroxidase Centre in Bacterioferritin.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Article
- Iron Oxidation inAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Article
- Iron Oxidation in Escherichia coli Bacterioferritin Ferroxidase Centre, a Site Designed to React Rapidly with HAngewandte Chemie (International ed. in English) · 2021Article
- Electron Transfer from Haem to the Di-Iron Ferroxidase Centre in Bacterioferritin.Angewandte Chemie (International ed. in English) · 2021Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Mobilization of iron stored in the interior cavity of BfrB requires electron transfer from the [2Fe−2S] cluster in Bfd to the core iron in BfrB. A crystal structure of the Pseudomonas aeruginosa BfrB:Bfd complex revealed that BfrB can bind up to 12 Bfd molecules at 12 structurally identical binding sites, placing the [2Fe−2S] cluster of each Bfd immediately above a heme group in BfrB [Yao, H., et al. (2012) J. Am. Chem. Soc., 134, 13470−13481]. We report here study aimed at characterizing the strength of the P. aeruginosa BfrB:Bfd association using surface plasmon resonance and isothermal titration calorimetry as well as determining the binding energy hot spots at the protein−protein interaction interface. The results show that the 12 Bfd-binding sites on BfrB are equivalent and independent and that the protein−protein association at each of these sites is driven entropically and is characterized by a dissociation constant (Kd) of approximately 3 μM. Determination of the binding energy hot spots was carried out by replacing certain residues that comprise the protein−protein interface with alanine and by evaluating the effect of the mutation on Kd and on the efficiency of core iron mobilization from BfrB. The results identified hot spot residues in both proteins [LB 68, EA 81, and EA 85 in BfrB (superscript for residue number and subscript for chain) and Y2 and L5 in Bfd] that network at the interface to produce a highly complementary hot region for the interaction. The hot spot residues are conserved in the amino acid sequences of Bfr and Bfd proteins from a number of Gram-negative pathogens, indicating that the BfrB:Bfd interaction is of widespread significance in bacterial iron metabolism.
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