Structural heterogeneity of pseudomonas aeruginosa bacterioferritin

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Moore, G. R., Kadir, F. H. A., Al-Massad, F. K., Le Brun, N. E., Thomson, A. J., Greenwood, C., Keen, J. N. and Findlay, J. B. C. (1994) Structural heterogeneity of pseudomonas aeruginosa bacterioferritin. Biochemical Journal, 304 (2). pp. 493-497. ISSN 0264-6021

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Abstract

The subunit composition, amino acid sequence and haem-binding characteristics of bacterioferritin (BFR) from Pseudomonas aeruginosa have been studied. Unlike other BFRs, P. aeruginosa BFR was found to contain two subunit types, designated α and β, which differed considerably in their amino acid sequences. The N-terminal 69 and 55 amino acids of the α and β subunits respectively were determnined. The α subunit differed most from other BFRs. The two subunits were present in variable proportions in different preparations. The maximum stoichiometry of haem binding was found to be sample-dependent and to be different from the previously reported one per subunit. This previous haem-binding study was shown to have been carried out with damaged protein, which contained both normal α and β subunits and shorter versions of these that appeared to have been produced by cleavage of the normal subunits. The possibility that aging processes degrade ferritins and affect their haem-binding characteristics is discussed.

Item Type:	Article
Uncontrolled Keywords:	biochemistry,molecular biology,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1303
Faculty \ School:	Faculty of Science > School of Chemistry (former - to 2024) Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemistry of Life Processes
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	18 Jun 2025 09:30
Last Modified:	23 Jun 2025 10:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/99615
DOI:	10.1042/bj3040493

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