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An EPR investigation of non‐haem iron sites in Escherichia coli bacterioferritin and their interaction with phosphate
Author(s) -
Le Brun Nick E.,
Cheesman Myles R.,
Thomson Andrew J.,
Moore Geoffrey R.,
Andrews Simon C.,
Guest John R.,
Harrison Pauline M.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81353-2
Subject(s) - electron paramagnetic resonance , chemistry , escherichia coli , phosphate , dimer , crystallography , biochemistry , nuclear magnetic resonance , organic chemistry , physics , gene
EPR studies of bacterioferritin (BFR), an iron‐storage protein of Escherichia coli [1993, Biochem. J. 292, 47‐56.], have revealed the presence of non‐haem iron (III) (NHI) sites within the protein coat which may be involved in iron uptake and release. When nitric oxide was used as an EPR spin probe of the Fe(II) state of the NHI sites, two distinct mononuclear NHI species were found. Under certain conditions, an iron dimer was also observed. The reaction of phosphate with NHI species has been investigated. Results point to a function for this anion in core nucleation.