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Literature summary for 1.16.3.1 extracted from

  • Lawson, T.L.; Crow, A.; Lewin, A.; Yasmin, S.; Moore, G.R.; Le Brun, N.E.
    Monitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopy (2009), Biochemistry, 48, 9031-9039.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli to create mutants by site-directed mutagenesis Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
W133F protein is lesser sensitive to Fe2+ than wild-type protein Escherichia coli
W35F fluorescence spectrum is blunted compared to wild-type protein Escherichia coli
W35F/W133F oxidation of Fe2+ to Fe3+ is slightly reduced Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Zn2+ 50 Zn2+ ions per bacterioferritin blocked binding of Fe2+ Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABD3 strain JM109 and strain BL21(DE3)pLysS
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Subunits

Subunits Comment Organism
24-mer BFR consists of 24 identical subunits arranged as 12 subunit dimers, each dimer contains a ferroxidase center, X-ray diffraction Escherichia coli

Synonyms

Synonyms Comment Organism
BFR
-
Escherichia coli
ferroxidase center of bacterioferritin
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Escherichia coli