ArticleJournal of the American Chemical Society2012
The structure of the BfrB-Bfd complex reveals protein-protein interactions enabling iron release from bacterioferritin.
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 54 papers.
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Who cites it
54 citing papers in PubMed, 102 citations in OpenAlex.
- Influence of heme and pH on the oligomeric states of Brucella melitensis bacterioferritin.Acta crystallographica. Section D, Structural biology · 2026Article
- A permeable protein nanocage enables facile cargo loading and cytosolic protein delivery.Nature communications · 2026Article
- Inhibiting Bacterioferritin Iron Release Induces Iron Starvation and Metabolic Downshift, Potentiating Aminoglycosides inACS infectious diseases · 2026Article
- Structural Analysis and Inhibitor Modeling of Bacterioferritin From Brucella abortus.Proteins · 2026Article
- A permeable protein nanocage enables facile cargo loading and cytosolic protein delivery.bioRxiv : the preprint server for biology · 2026Article
- Metal-independent effects of calprotectin on cocultures ofbioRxiv : the preprint server for biology · 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
- Genome mining based on transcriptional regulatory networks uncovers a novel locus involved in desferrioxamine biosynthesis.PLoS biology · 2025Article
- Unveiling Structural Heterogeneity and Evolutionary Adaptations of Heteromultimeric Bacterioferritin Nanocages.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Molybdate uptake interplay with ROS tolerance modulates bacterial pathogenesis.Science advances · 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
- Iron mobilization from intact ferritin: effect of differential redox activity of quinone derivatives with NADH/OJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Article
- In Silico Drug Repurposing Studies for the Discovery of Novel Salicyl-AMP Ligase (MbtA)Inhibitors.Pathogens (Basel, Switzerland) · 2023Article
- Mobilization of iron stored in bacterioferritin, a new target for perturbing iron homeostasis and developing antibacterial and antibiofilm molecules.Journal of inorganic biochemistry · 2023Review
- Dps Functions as a Key Player in Bacterial Iron Homeostasis.ACS omega · 2023Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Ferritin-like molecules are unique to cellular iron homeostasis because they can store iron at concentrations much higher than those dictated by the solubility of Fe(3+). Very little is known about the protein interactions that deliver iron for storage or promote the mobilization of stored iron from ferritin-like molecules. Here, we report the X-ray crystal structure of Pseudomonas aeruginosa bacterioferritin (Pa-BfrB) in complex with bacterioferritin-associated ferredoxin (Pa-Bfd) at 2.0 Å resolution. As the first example of a ferritin-like molecule in complex with a cognate partner, the structure provides unprecedented insight into the complementary interface that enables the [2Fe-2S] cluster of Pa-Bfd to promote heme-mediated electron transfer through the BfrB protein dielectric (~18 Å), a process that is necessary to reduce the core ferric mineral and facilitate mobilization of Fe(2+). The Pa-BfrB-Bfd complex also revealed the first structure of a Bfd, thus providing a first view to what appears to be a versatile metal binding domain ubiquitous to the large Fer2_BFD family of proteins and enzymes with diverse functions. Residues at the Pa-BfrB-Bfd interface are highly conserved in Bfr and Bfd sequences from a number of pathogenic bacteria, suggesting that the specific recognition between Pa-BfrB and Pa-Bfd is of widespread significance to the understanding of bacterial iron homeostasis.
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