Cellular and Molecular Life Sciences CMLS

, Volume 57, Issue 13, pp 1909–1926

Ferrochelatase at the millennium: structures, mechanisms and [2Fe-2S] clusters

  • H. A. Dailey*
  • T. A. Dailey
  • C.-K. Wu**
  • A. E. Medlock
  • J. P. Rose
  • K.-F. Wang

DOI: 10.1007/PL00000672

Cite this article as:
Dailey*, H., Dailey, T., Wu**, CK. et al. CMLS, Cell. Mol. Life Sci. (2000) 57: 1909. doi:10.1007/PL00000672
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Abstract.

Ferrochelatase (E.C. 4.99.1.1, protoheme ferrolyase) catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme (heme). In the past 2 years, the crystal structures of ferrochelatases from the bacterium Bacillus subtilis and human have been determined. These structures along with years of biophysical and kinetic studies have led to a better understanding of the catalytic mechanism of ferrochelatase. At present, the complete DNA sequences of 45 ferrochelatases from procaryotes and eucaryotes are available. These sequences along with direct protein studies reveal that ferrochelatases, while related, vary significantly in amino acid sequence, molecular size, subunit composition, solubility, and the presence or absence of nitric-oxide-sensitive [2Fe-2S] cluster.

Key words. Ferrochelatase; heme synthesis; iron sulfur cluster; metallation; porphyria. 

Copyright information

© Birkhäuser Verlag Basel, 2000

Authors and Affiliations

  • H. A. Dailey*
    • 1
  • T. A. Dailey
    • 1
  • C.-K. Wu**
    • 1
  • A. E. Medlock
    • 1
  • J. P. Rose
    • 1
  • K.-F. Wang
    • 1
  1. 1.Department of Biochemistry and Molecular Biology, and Department of Microbiology, University of Georgia, Athens (Georgia 30605-7229, USA), Fax +1 706 542 7567, e-mail: hdailey@arches.uga.edu US

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