Charge compensated binding of divalent metals to bacterioferritin:H+ release associated with cobalt(II) and zinc(II) binding at dinuclear metal sites

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Le Brun, Nick E., Keech, Angus M., Mauk, Marcia R., Mauk, A. Grant, Andrews, Simon C., Thomson, Andrew J. and Moore, Geoffrey R. (1996) Charge compensated binding of divalent metals to bacterioferritin:H+ release associated with cobalt(II) and zinc(II) binding at dinuclear metal sites. FEBS Letters, 397 (2-3). pp. 159-163. ISSN 0014-5793

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Abstract

Divalent metal ion binding to the bacterial iron-storage protein, bacterioferritin (BFR), which contains a dinuclear metal binding site within each of its 24 subunits, was investigated by potentiometric and spectrophotometric methods. Cobalt(II) and zinc(II) were found to bind at both high- and low-affinity sites. Cobalt(II) binding at the high-affinity site was observed at a level of two per subunit with the release of ~1.6 protons per metal ion, thus confirming the dinuclear metal centre as the high-affinity site. Zinc(II) binding at the dinuclear centre (high-affinity site) resulted in the release of ~2 protons per metal ion, but exhibited a binding stoichiometry which indicated that not all dinuclear centres were capable of binding two zinc(II) ions. Competition data showed that binding affinities for the dinuclear centre were in the order zinc(II) > cobalt(II), and also confirmed the unexpected stoichiometry of zinc(II) binding. This work emphasises the importance of charge neutrality at the dinuclear centre.

Item Type:	Article
Uncontrolled Keywords:	bacterioferritin,charge neutrality,cobalt(ii),dinuclear center,potentiometry,zinc(ii),biophysics,structural biology,biochemistry,molecular biology,genetics,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1304
Faculty \ School:	Faculty of Science > School of Chemistry (former - to 2024)
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:	24 Jun 2025 13:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/99610
DOI:	10.1016/S0014-5793(96)01172-6

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