Results 181 to 190 of about 4,768 (212)
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Metal Inhibition of Ferrochelatase
Annals of the New York Academy of Sciences, 1987Ferrochelatase activity was examined both in growing MEL cells and in in vitro assays of the purified enzyme to determine what effect a variety of divalent cations would have. Data obtained with the purified enzyme demonstrated that Mn2+ strongly inhibits the activity in a competitive fashion with respect to Fe2+ with a calculated Ki of 15 microM ...
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Proteobacteria-like ferrochelatase in the malaria parasite
Current Genetics, 2003A gene encoding the heme biosynthetic enzyme ferrochelatase (FC) was found in the genomic DNA databases of Plasmodium spp. The predicted amino acid sequence of malarial FC is highly conserved and fairly well conserved by comparison with other orthologues. The FC genes of P. falciparum and P.
Shigeharu, Sato, R J M, Wilson
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Orientation of ferrochelatase in bovine liver mitochondria
Biochemistry, 1985The orientation of ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1), the terminal enzyme of the heme biosynthetic pathway, was examined in bovine liver mitochondria. The ability of a membrane-impermeable sulfhydryl reagent, 4,4'-dimaleimidylstilbene-2,2'-disulfonic acid, to inactivate ferrochelatase in intact or disrupted mitochondria and mitoplasts
B M, Harbin, H A, Dailey
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Protoporphyrinogen oxidase and ferrochelatase in porphyria variegata
European Journal of Clinical Investigation, 1983Abstract. Protoporphyrinogen oxidase activity and ferrochelatase activity were measured in leucocytes from patients with porphyria variegata. The mean activity of protoporphyrinogen oxidase (PPO) in porphyria variegata (PV) was about 50% of normal (P < 0.05). The mean activity of ferrochelatase with 59Fe2+ sulphate and protoporphyrin as substrates (
D J, Viljoen +3 more
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Human ferrochelatase is an iron-sulfur protein
Biochemistry, 1994Recombinant human ferrochelatase has been expressed in Escherichia coli and purified to homogeneity. Metal analyses revealed approximately 2 mol of non-heme Fe per mol of the purified enzyme (M(r) = 40,000). The UV-visible absorption spectrum of the purified enzyme consists of a protein absorption at 278 nm (epsilon approximately 90,000 M-1 cm-1) and ...
H A, Dailey, M G, Finnegan, M K, Johnson
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2010
Regulatory factors affecting ferrochelatase activity were studied and an attempt was made to determine the role of ferrochelatase in the regulation of heme biosynthesis. Ferrochelatase was found to have a Km value of 0.105 mM for the porphyrin substrates, proto and mesoporphyrin IX and a Km value of 8.30 x 10⁻³ mM for ferrous ion, its metal substrate ...
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Regulatory factors affecting ferrochelatase activity were studied and an attempt was made to determine the role of ferrochelatase in the regulation of heme biosynthesis. Ferrochelatase was found to have a Km value of 0.105 mM for the porphyrin substrates, proto and mesoporphyrin IX and a Km value of 8.30 x 10⁻³ mM for ferrous ion, its metal substrate ...
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Deletion of the ferrochelatase gene in a patient with protoporphyria
Human Molecular Genetics, 19941697
Magness, Scott T. +6 more
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Regulation of ferrochelatase gene expression by hypoxia
Life Sciences, 2004Ferrochelatase (FECH), the last enzyme of the heme biosynthetic pathway, catalyzes the insertion of iron into protoporphyrin to form heme. This pathway provides heme for hemoglobin and other essential hemoproteins. The regulatory role of oxygen in the pathway has not been clearly established.
Yunying L, Liu +4 more
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Characterization of ferrochelatase in kidney and erythroleukemia cells
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990Ferrochelatase from bovine kidney mitochondria has been purified 1600-fold with a 6.5% yield, exhibiting a specific activity of 490 nmol mesoheme formed/mg of protein per min. The Km values for mesoporphyrin IX and protoporphyrin IX with iron were 12.5 and 12.7 microM, respectively.
Y, Nakahashi +3 more
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Metal ion coordination sites in ferrochelatase
Coordination Chemistry Reviews, 2022Gloria C Ferreira
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