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. 1974 Jun;139(3):709–714. doi: 10.1042/bj1390709

Iron and aconitase activity

Oscar Gawron 1,*, Abdul Waheed 1, Andrew J Glaid III 1, Anna Jaklitsch 1
PMCID: PMC1166334  PMID: 4852570

Abstract

Aconitase activated with Fe2+, cysteine and ascorbate incorporates 1 g-atom of Fe2+/mol. Loss of this Fe2+ by transfer to ferrozine, a Fe2+ chelator, results in loss of activity. Ascorbate increases the rate of transfer of the essential Fe2+ whereas citrate retards the rate of transfer. Transfer of Fe2+ from inactive aconitase, 2 g-atoms of Fe/mol, can be accomplished in the presence of urea and ascorbate. The correlation of activity with the presence of an added g-atom of Fe2+/mol leads to the conclusion that active aconitase has only one active site per mol.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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