Abstract
Iron is no less an essential element to most microbes than it is to higher organisms. Iron uptake systems and their regulation in Escherichia coli are relatively well characterized1 and the importance of many microbial iron-containing molecules, for example, the cytochromes2, is well established. Just over ten years ago the presence of a ferritin-like molecule was reported in Azotohacter vinelandii 3 and E. coli 4. It was considered to be ferritin-like in that it had an electron-dense iron-containing core with a protein coat of similar dimensions to those of mammalian ferritin. The two types of ‘ferritin’ had rather similar amino acid compositions and their non-haem iron-cores were of low redox potential, but the ‘bacterioferritins’ were distinguished by the presence of protoporphyrin IX. The bacterioferritin (BFR) of A. vinelandii was shown to be identical to the non-haem iron-containing cytochrome b 557.5 previously isolated by Bulen and co-workers5 and that from E. coli to the cytochrome b 1 described by Deeb and Hager6 and Fujita et al 7. Similar molecules have been isolated from Pseudomonas aeruginosa 8, A. chroococcum 9 and from Nitrobacter winogradskyi 10 Despite their resemblance to ferritin, the physiological role of these molecules in bacteria has not been established, but in vitro they are able to sequester iron11.
An erratum to this chapter is available at http://dx.doi.org/10.1007/978-1-4615-3810-3_32
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Smith, J.M.A., Andrews, S.C., Guest, J.R., Harrison, P.M. (1991). Bacterioferritin: A Microbial Iron-Storage Protein?. In: Frankel, R.B., Blakemore, R.P. (eds) Iron Biominerals. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3810-3_23
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