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

• Published in: Cellular and molecular life sciences : CMLS 2000-12, Vol.57 (13-14), p.1909-1926
• Main Authors: Dailey, H A, Dailey, T A, Wu, C K, Medlock, A E, Wang, K F, Rose, J P, Wang, B C
• Format: Article
• Language: English
• Subjects: Amino acid composition; Amino Acid Sequence; Amino acids; Animals; Crystal structure; Crystallography, X-Ray; Evolution, Molecular; Ferrochelatase; Ferrochelatase - chemistry; Ferrochelatase - genetics; Ferrochelatase - metabolism; Gene sequencing; Heme; Humans; Iron-Sulfur Proteins - chemistry; Iron-Sulfur Proteins - genetics; Iron-Sulfur Proteins - metabolism; Models, Molecular; Molecular Sequence Data; Nitric oxide; Nucleotide sequence; Phylogeny; Porphyria, Hepatoerythropoietic - enzymology; Porphyria, Hepatoerythropoietic - genetics; Protein Conformation; Protoporphyrin; Protoporphyrin IX; Sequence Alignment; Structure-Activity Relationship; Subunit structure
• ISSN: 1420-682X; 1420-9071
• DOI: 10.1007/pl00000672

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.