Two Distinct Ferritin-like Molecules in Pseudomonas aeruginosa: The Product of the bfrA Gene Is a Bacterial Ferritin (FtnA) and Not a Bacterioferritin (Bfr)
H Yao, G Jepkorir, S Lovell, PV Nama… - Biochemistry, 2011 - ACS Publications
Two distinct types of ferritin-like molecules often coexist in bacteria, the heme binding
bacterioferritins (Bfr) and the non-heme binding bacterial ferritins (Ftn). The early isolation of …
bacterioferritins (Bfr) and the non-heme binding bacterial ferritins (Ftn). The early isolation of …
Unification of the ferritin family of proteins.
MJ Grossman, SM Hinton… - Proceedings of the …, 1992 - National Acad Sciences
Ferritin is the iron-storage protein of eukaryotic organisms. The nucleotide sequence
encoding Azotobacter vinelandii bacterioferritin, a hemoprotein, was determined. The …
encoding Azotobacter vinelandii bacterioferritin, a hemoprotein, was determined. The …
Overproduction, purification and characterization of the bacterioferritin of Escherichia coli and a C‐terminally extended variant
SC Andrews, JMA SMITH, C Hawkins… - European journal of …, 1993 - Wiley Online Library
The bacterioferritin (BFR) of Escherichia coli is an iron‐sequestering haemoprotein
composed of 24 identical polypeptide chains forming an approximately spherical protein …
composed of 24 identical polypeptide chains forming an approximately spherical protein …
Spectroscopic and Voltammetric Characterisation of the Bacterioferritin-Associated Ferredoxin ofEscherichia coli
MA Quail, P Jordan, JM Grogan, JN Butt, M Lutz… - Biochemical and …, 1996 - Elsevier
Thebacterioferritin-associatedferredoxin (Bfd) ofEscherichia coliis a 64-residue polypeptide
encoded by thebfdgene located upstream of the gene (bfr) encoding the iron-storage …
encoded by thebfdgene located upstream of the gene (bfr) encoding the iron-storage …
A [2Fe-2S] Protein Encoded by an Open Reading Frame Upstream of the Escherichia coli Bacterioferritin Gene†
RP Garg, CJ Vargo, X Cui, DM Kurtz - Biochemistry, 1996 - ACS Publications
An open reading frame located upstream of the bacterioferritin gene in Escherichia coli
encodes a hypothetical 64-residue protein [Andrews, SC, Harrison, PC, & Guest, JR (1989) …
encodes a hypothetical 64-residue protein [Andrews, SC, Harrison, PC, & Guest, JR (1989) …
Analysis of eight out genes in a cluster required for pectic enzyme secretion by Erwinia chrysanthemi: sequence comparison with secretion genes from other gram …
M Lindeberg, A Collmer - Journal of bacteriology, 1992 - Am Soc Microbiol
Many extracellular proteins produced by Erwinia chrysanthemi require the out gene
products for transport across the outer membrane. In a previous report (SY He, M …
products for transport across the outer membrane. In a previous report (SY He, M …
Identification of the ferroxidase centre of Escherichia coli bacterioferritin
NE Le Brun, SC Andrews, JR Guest… - Biochemical …, 1995 - portlandpress.com
The bacterioferritin (BFR) of Escherichia coli takes up iron in the ferrous form and stores it
within its central cavity as a hydrated ferric oxide mineral. The mechanism by which …
within its central cavity as a hydrated ferric oxide mineral. The mechanism by which …
Purification, characterization, gene sequence, and significance of a bacterioferritin from Mycobacterium leprae.
MC Pessolani, DR Smith, B Rivoire… - The Journal of …, 1994 - rupress.org
The study of tissue-derived Mycobacterium leprae provides insights to the immunopathology
of leprosy and helps identify broad molecular features necessary for mycobacterial …
of leprosy and helps identify broad molecular features necessary for mycobacterial …
Characterization of the bacterioferritin/bacterioferritin associated ferredoxin protein–protein interaction in solution and determination of binding energy hot spots
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 …
2S] cluster in Bfd to the core iron in BfrB. A crystal structure of the Pseudomonas aeruginosa …
The haemoglobin‐like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C‐terminal domain shares homology with ferredoxin NADP+ …
SC Andrews, D Shipley, JN Keen, JBC Findlay… - FEBS …, 1992 - Wiley Online Library
Three soluble ferrisiderophore reductases (FsrA, FsrB and FsrC) were detected in
Escherichia coli. FsrB was purified and identified as the haemoglobin‐like protein (HMP) by …
Escherichia coli. FsrB was purified and identified as the haemoglobin‐like protein (HMP) by …