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

Research output: Contribution to journalReview articlepeer-review

151 Scopus citations


Ferrochelatase (E.C., 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.

Original languageEnglish (US)
Pages (from-to)1909-1926
Number of pages18
JournalCellular and Molecular Life Sciences
Issue number13-14
StatePublished - 2000


  • Ferrochelatase
  • Heme synthesis
  • Iron sulfur cluster
  • Metallation
  • Porphyria

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology


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