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Structure and function of ferrochelatase
Journal of Bioenergetics and Biomembranes, 1995Ferrochelatase is the terminal enzyme of the heme biosynthetic pathway in all cells. It catalyzes the insertion of ferrous iron into protoporphyrin IX, yielding heme. In eukaryotic cells, ferrochelatase is a mitochondrial inner membrane-associated protein with the active site facing the matrix. Decreased values of ferrochelatase activity in all tissues
G C, Ferreira +5 more
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BBA - Proteins and Proteomics, 1989
The ability of purified mouse ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1) to bind and catalytically utilize a variety of porphyrins has been examined. In all, the kd, Km or Ki values for eleven different porphyrins, the Ki values for four metalloporphyrins and the kd values for two metalloporphyrins were determined.
Harry A. Dailey
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The ability of purified mouse ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1) to bind and catalytically utilize a variety of porphyrins has been examined. In all, the kd, Km or Ki values for eleven different porphyrins, the Ki values for four metalloporphyrins and the kd values for two metalloporphyrins were determined.
Harry A. Dailey
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Properties of the Cobaltochelatase and the Ferrochelatase
Enzyme, 2017The formation of cobaltomesoporphyrin and ferromesoporphyrin in the presence of appropriate chelatases has been studied. The K(m) value for mesoporphyrin differs for the two activities, although the optimum pH value is 8.1 for both. At high cobalt concentrations a slight non-enzymatic reaction occurs which is not seen with ferrous salts.
E T, Canepa, E B, Llambias
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Molecular and Cellular Biochemistry, 2004
All organisms utilize ferrochelatase (EC 4.99.1.1) to catalyze the insertion of ferrous iron into protoposphyrin IX in the terminal step of the heme biosynthetic pathway. Different metal-binding affinity for the enzyme leads to changes in enzyme activity. In this work, we have cloned and over-expressed the enzyme from chironomidae in E. coli.
Yuet Kin, Leung +3 more
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All organisms utilize ferrochelatase (EC 4.99.1.1) to catalyze the insertion of ferrous iron into protoposphyrin IX in the terminal step of the heme biosynthetic pathway. Different metal-binding affinity for the enzyme leads to changes in enzyme activity. In this work, we have cloned and over-expressed the enzyme from chironomidae in E. coli.
Yuet Kin, Leung +3 more
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The International Journal of Biochemistry & Cell Biology, 1999
Ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous iron into protoporphyrin IX. It is encoded by a single gene, and mutations in the human gene are associated with the inherited disorder, erythropoietic protoporphyria.
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Ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous iron into protoporphyrin IX. It is encoded by a single gene, and mutations in the human gene are associated with the inherited disorder, erythropoietic protoporphyria.
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Saccharomyces cerevisiae Ferrochelatase Forms a Homodimer
Archives of Biochemistry and Biophysics, 2002Ferrochelatase, the last enzyme of the heme biosynthetic pathway, has for years been considered to be active as a monomer. The crystal structure of Bacillus subtilis ferrochelatase confirmed its monomeric structure. However, animal ferrochelatase was found to form a functional dimer.
Monika Gora +2 more
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QM/MM Study of the Insertion of Metal Ion Into Protoporphyrin IX by Ferrochelatase
Journal of Inorganic Biochemistry, 2009 Ferrochelatase catalyzes the metallation of protoporphyrin IX in the terminal step of heme biosynthesis. Mutations in the ferrochelatase gene can lead to the disease erythropoietic porphyria.
Ulf Ryde, Yaxue Wang, Yong Shen
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Measurement of Ferrochelatase Activity
Current Protocols in Toxicology, 1999AbstractFerrochelatase is the terminal enzyme in the heme biosynthesis pathway. Under anaerobic conditions it catalyzes the insertion of ferrous iron into the protoporphyrin IX ring to form protoheme. In the absence of iron and under aerobic conditions, the enzyme will use zinc or mercury as a substitute.
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Effects of lipids on the activity of ferrochelatase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1977Removal of lipids from submitochondrial particles or detergent-solubilized mitochondrial preparations of rat liver resulted in a 90% loss of ferrochelatase (protochemeferro-lyase, EC 4.99.1.1) activity. The addition of either a fatty acid or phospholipid restored enzyme activity; the extent of reactivation being correlated with the degree of ...
D M, Simpson, R, Poulson
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Ferrochelatase and N-alkylated porphyrins
Molecular and Cellular Biochemistry, 1984The final step in heme synthesis is catalyzed by the mitochondrial enzyme, ferrochelatase. Characterization of this enzyme has been complicated by a number of factors including the dependence of enzyme activity on lipids. Purification of ferrochelatase from rat and bovine sources has been achieved only relatively recently using blue Sepharose CL-6B ...
S P, Cole, G S, Marks
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