PMID:8954950

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Citation

Quail, MA, Jordan, P, Grogan, JM, Butt, JN, Lutz, M, Thomson, AJ, Andrews, SC and Guest, JR (1996) Spectroscopic and voltammetric characterisation of the bacterioferritin-associated ferredoxin of Escherichia coli. Biochem. Biophys. Res. Commun. 229:635-42

Abstract

The bacterioferritin-associated ferredoxin (Bfd) of Escherichia coli is a 64-residue polypeptide encoded by the bfd gene located upstream of the gene (bfr) encoding the iron-storage haemoprotein, bacterioferritin. The Bfd sequence resembles those of the approximately 60-residue domains found in NifU proteins (required for metallocluster assembly), nitrite reductases, and Klebsiella pneumoniae nitrate reductase. These related-domains contain four well-conserved cysteine residues, which are thought to function as ligands to a [2Fe-2S] cluster. The Bfd protein was over-produced, purified, and characterised. Bfd was found to be a positively-charged monomer containing two iron atoms and two labile sulphides. Ultraviolet-visible, EPR, variable-temperature magnetic-circular dichroism and resonance Raman spectroscopies, together with cyclic voltogram measurements, revealed the presence of a [2Fe-2S]2+,+ centre (E1/2 = -254 mV) having remarkably similar properties to the Fe-S cluster of NifU. Bfd may thus be a 2Fe ferredoxin participating either in release/delivery of iron from/to bacterioferritin (or other iron complexes), or in iron-dependent regulation of bfr expression.

Links

PubMed Online version:10.1006/bbrc.1996.1856

Keywords

Amino Acid Sequence; Bacterial Proteins; Cytochrome b Group/chemistry; Cytochrome b Group/genetics; Cytochrome b Group/isolation & purification; Electrochemistry; Escherichia coli/chemistry; Ferredoxins/chemistry; Ferritins/chemistry; Ferritins/genetics; Ferritins/isolation & purification; Glutathione Transferase/genetics; Molecular Sequence Data; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/isolation & purification; Spectrum Analysis

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