Iron binding and autoreduction by citrate: are these involved in signalling by iron regulatory protein-1?

Ferric ions bind to citrate and undergo an autoreduction to form a ferrous-citrate complex, greatly increasing the redox activity of the iron complex. Ferrous ions and citrate are also essential for the enzymic activity of aconitase. Aconitase, with its iron-sulphur cluster has a versatile structure...

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Veröffentlicht in:Free radical research 1998-03, Vol.28 (3), p.319-322
Hauptverfasser: Gutteridge, J M, Mumby, S, Lamb, N J
Format: Artikel
Sprache:eng
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Zusammenfassung:Ferric ions bind to citrate and undergo an autoreduction to form a ferrous-citrate complex, greatly increasing the redox activity of the iron complex. Ferrous ions and citrate are also essential for the enzymic activity of aconitase. Aconitase, with its iron-sulphur cluster has a versatile structure which allows it to act as an iron regulatory protein (IRP-1). The purpose of this study was to see whether iron binding, and its autoreduction by citrate, could play a physiological signalling role in iron regulation. Significant amounts of ferrous ions were associated with citrate, when measured using ferrozine, however, these did not appear to activate iron-requiring aconitase.
ISSN:1071-5762
DOI:10.3109/10715769809069283