Ferrochelatase a new iron sulfur center-containing enzyme

Ricardo Franco, Steven G. Lloyd, Jose J. G. Moura, Isabel Moura, Boi Hanh Huynh and Gloria C. Ferreira 

Hie expression of recombinant mammalian liver ferrochelatases in Escherichia coli [4, 5], allowed the production of increased amounts of the enzyme and led to the unexpected discovery of a [2Fe-2S] cluster in the mammalian enzymes (mouse [6] and human [7]). The large amoimts of protein made available using heterologous over-producing systems allowed detailed spectroscopic studies on the cluster-containing ferrochelatases. Yeast Saccharomyces cerevisiae) ferrochelatase, which is devoid of an iron-sulfur cluster, has also been extensively studied and several site-directed mutants have been produced [8], making it a powerful model system to study the mechanism of this enzyme. 

In this chapter we will review the present knowledge of ferrochelatase in terms of its structure and function, with special emphasis on the mammalian enzymes and their intriguing [2Fe-2S] cluster. 

3 Ferrochelatase a new iron sulfur center-containing enzyme 

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