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Ferrochelatase at the millennium: structures, mechanisms and [2Fe-2S] clusters
H A Dailey1, T A Dailey, C K Wu
1Department of Biochemistry and Molecular Biology, University of Georgia, Athens 30605-7229, USA. hdailey@arches.uga.edu
Cellular and Molecular Life Sciences : CMLS
|February 24, 2001
Summary
Ferrochelatase, an enzyme essential for heme synthesis, has had its structure elucidated through recent crystallographic studies. This research deepens our understanding of its catalytic mechanism and variations across species.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Ferrochelatase (E.C. 4.99.1.1) catalyzes the final step in heme biosynthesis: the insertion of ferrous iron into protoporphyrin IX.
- Heme is crucial for various cellular functions, including oxygen transport and electron transfer.
Purpose of the Study:
- To elucidate the catalytic mechanism of ferrochelatase.
- To understand structural variations of ferrochelatase across different organisms.
Main Methods:
- X-ray crystallography of Bacillus subtilis and human ferrochelatases.
- Biophysical and kinetic studies.
- Comparative analysis of 45 available ferrochelatase DNA sequences.
Main Results:
- Crystal structures of bacterial and human ferrochelatases have been determined.
- Sequence analysis reveals significant variations in amino acid sequence, molecular size, subunit composition, and solubility among ferrochelatases.
- The presence or absence of a nitric-oxide-sensitive [2Fe-2S] cluster is a notable variation.
Conclusions:
- Recent structural and sequence data provide a comprehensive understanding of ferrochelatase's catalytic mechanism.
- Ferrochelatases exhibit considerable diversity, impacting their biochemical properties and potential functions.
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