Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 57, Issue 13-14, Pages 1909-1926Publisher
SPRINGER BASEL AG
DOI: 10.1007/PL00000672
Keywords
ferrochelatase; heme synthesis; iron sulfur cluster; metallation; porphyria
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Funding
- NIDDK NIH HHS [DK 32303, R56 DK032303] Funding Source: Medline
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Ferrochelatase (E.C. 4.99.1.1, protoheme ferrolyase) catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme theme). 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.
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