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  • Title: An EPR investigation of non-haem iron sites in Escherichia coli bacterioferritin and their interaction with phosphate. A study using nitric oxide as a spin probe.
    Author: Le Brun NE, Cheesman MR, Thomson AJ, Moore GR, Andrews SC, Guest JR, Harrison PM.
    Journal: FEBS Lett; 1993 Jun 01; 323(3):261-6. PubMed ID: 8388809.
    Abstract:
    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.
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