A new class of [2Fe-2S]-cluster-containing protoporphyrin (IX) ferrochelatases.

Shepherd, Mark and Dailey, Tamara A. and Dailey, Harry A. (2006) A new class of [2Fe-2S]-cluster-containing protoporphyrin (IX) ferrochelatases. Biochemical Journal, 397 (1). pp. 47-52. ISSN 0264-6021. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Protoporphyrin (IX) ferrochelatase catalyses the insertion of ferrous iron into protoporphyrin IX to form haem. These ferrochelatases exist as monomers and dimers, both with and without [2Fe-2S] clusters. The motifs for [2Fe-2S] cluster co-ordination are varied, but in all cases previously reported, three of the four cysteine ligands are present in the 30 C-terminal residues and the fourth ligand is internal. In the present study, we demonstrate that a group of micro-organisms exist which possess protoporphyrin (IX) ferrochelatases containing [2Fe-2S] clusters that are co-ordinated by a group of four cysteine residues contained in an internal amino acid segment of approx. 20 residues in length. This suggests that these ferrochelatases have evolved along a different lineage than other bacterial protoporphyrin (IX) ferrochelatases. For example, Myxococcus xanthus protoporphyrin (IX) ferrochelatase ligates a [2Fe-2S] cluster via cysteine residues present in an internal segment. Site-directed mutagenesis of this ferrochelatase demonstrates that changing one cysteine ligand into serine results in loss of the cluster, but unlike eukaryotic protoporphyrin (IX) ferrochelatases, this enzyme retains its activity. These data support a role for the [2Fe-2S] cluster in iron affinity, and strongly suggest convergent evolution of this feature in prokaryotes.

Item Type: Article
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Mark Shepherd
Date Deposited: 01 Sep 2011 16:00
Last Modified: 15 Apr 2014 07:52
Resource URI: https://kar.kent.ac.uk/id/eprint/28097 (The current URI for this page, for reference purposes)
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