PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10858295-1 2000 Insertion of ferrous iron into protoporphyrin IX is catalyzed by ferrochelatase (EC 4.99.1.1). Iron 13-25 ferrochelatase Homo sapiens 65-79 10828045-1 2000 Ferrochelatase, the last enzyme in the heme pathway, chelates protoporphyrin IX and iron to form heme and is mutated in protoporphyria. Iron 84-88 ferrochelatase Homo sapiens 0-14 10561552-1 1999 Ferrochelatase (protoheme ferrolyase, EC 4.99.1.1) catalyzes the terminal step in the heme biosynthetic pathway, the insertion of ferrous iron into protoporphyrin IX to form protoheme IX. Iron 130-142 ferrochelatase Homo sapiens 0-14 11498837-13 1999 The level of intracellular iron in non-induced and induced MEL cells had less effects on the expression of ferrochelatase mRNA. Iron 27-31 ferrochelatase Homo sapiens 107-121 9989256-1 1999 Protoporphyria is a disease characterized by a deficiency in ferrochelatase, the terminal enzyme in the heme biosynthetic pathway, which catalyzes the chelation of iron and protoporphyrin to form heme. Iron 164-168 ferrochelatase Homo sapiens 61-75 10582332-1 1999 Ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous iron into protoporphyrin IX. Iron 97-109 ferrochelatase Homo sapiens 0-14 7592847-0 1995 Characterization of the iron-binding site in mammalian ferrochelatase by kinetic and Mossbauer methods. Iron 24-28 ferrochelatase Homo sapiens 55-69 9347801-1 1997 Human erythropoietic protoporphyria is an inherited disorder of the heme metabolic pathway caused by defects in the gene for ferrochelatase, the terminal enzyme of the pathway that catalyzes chelation of ferrous iron into protoporphyrin IX to form heme. Iron 204-216 ferrochelatase Homo sapiens 125-139 9740232-2 1998 Ferrochelatase catalyzes the chelation of ferrous iron into protoporphyrin IX to form heme. Iron 42-54 ferrochelatase Homo sapiens 0-14 9639532-1 1998 Ferrochelatase catalyzes the chelation of ferrous iron and protoporphyrin to form heme. Iron 42-54 ferrochelatase Homo sapiens 0-14 7575558-0 1995 Ferrochelatase binds the iron-responsive element present in the erythroid 5-aminolevulinate synthase mRNA. Iron 25-29 ferrochelatase Homo sapiens 0-14 7544575-0 1995 Nitric oxide-mediated inactivation of mammalian ferrochelatase in vivo and in vitro: possible involvement of the iron-sulphur cluster of the enzyme. Iron 113-117 ferrochelatase Homo sapiens 48-62 7857832-1 1994 Erythropoietic protoporphyria (EPP) is an inherited inborn error of porphyrin metabolism caused by decreased activity of the enzyme ferrochelatase, the terminal enzyme of the haem biosynthetic pathway, which catalyses the insertion of iron into protoporphyrin to form haem. Iron 235-239 ferrochelatase Homo sapiens 132-146 7544575-6 1995 These results indicate that ferrochelatase activity can be modulated by NO synthesis probably through disruption of the iron-sulphur cluster. Iron 120-124 ferrochelatase Homo sapiens 28-42 7712294-1 1994 The haem biosynthesis pathway continues to provide surprises, from the first enzyme, 5-aminolaevulinic acid synthase, the mRNA of which contains an iron-responsive element, to the last, ferrochelatase, that contains an iron sulphur cluster. Iron 219-223 ferrochelatase Homo sapiens 186-200 8276824-2 1994 Ferrochelatase (EC 4.99.1.1) catalyzes the terminal step in the heme biosynthetic pathway, the insertion of ferrous iron into protoporphyrin IX. Iron 108-120 ferrochelatase Homo sapiens 0-14 8031831-4 1994 Expressed ferrochelatase exhibited iron- and zinc-chelating activities, and was found as a soluble protein. Iron 35-39 ferrochelatase Homo sapiens 10-24 8308010-9 1994 Specifically, the recombinant ferrochelatase has iron and porphyrin as substrates, and N-methylprotoporphyrin and metal ions (e.g. Hg2+ and Mn2+), as strong inhibitors of its enzyme activity. Iron 49-53 ferrochelatase Homo sapiens 30-44 8276824-2 1994 Ferrochelatase (EC 4.99.1.1) catalyzes the terminal step in the heme biosynthetic pathway, the insertion of ferrous iron into protoporphyrin IX. Iron 108-120 ferrochelatase Homo sapiens 16-27 35309058-3 2022 Although several papers report the presence of iron deficiency anemia in about 50% of EPP patients, there is still no a conclusive explanation of the why this occurs. Iron 47-51 ferrochelatase Homo sapiens 86-89 8244265-1 1993 Protoporphyria is a genetic disorder characterized by a defect in the enzyme ferrochelatase, which catalyzes the chelation of iron to protoporphyrin. Iron 126-130 ferrochelatase Homo sapiens 77-91 8337255-4 1993 Porphyrin accumulation was enhanced by Ca Mg ethylenediaminetetraacetic acid, a ferrochelatase inhibitor, and the enhancement was reversed by the addition of iron, suggesting the utilization of iron by ferrochelatase. Iron 158-162 ferrochelatase Homo sapiens 202-216 8337255-4 1993 Porphyrin accumulation was enhanced by Ca Mg ethylenediaminetetraacetic acid, a ferrochelatase inhibitor, and the enhancement was reversed by the addition of iron, suggesting the utilization of iron by ferrochelatase. Iron 194-198 ferrochelatase Homo sapiens 202-216 34940556-4 2021 Moreover, it has been shown that the expression of ferrochelatase (FECH, an iron-sulfur cluster enzyme that inserts iron into protoporphyrin IX to form heme), is regulated by intracellular iron level. Iron 76-80 ferrochelatase Homo sapiens 51-65 34940556-4 2021 Moreover, it has been shown that the expression of ferrochelatase (FECH, an iron-sulfur cluster enzyme that inserts iron into protoporphyrin IX to form heme), is regulated by intracellular iron level. Iron 76-80 ferrochelatase Homo sapiens 67-71 34940556-4 2021 Moreover, it has been shown that the expression of ferrochelatase (FECH, an iron-sulfur cluster enzyme that inserts iron into protoporphyrin IX to form heme), is regulated by intracellular iron level. Iron 116-120 ferrochelatase Homo sapiens 51-65 34940556-4 2021 Moreover, it has been shown that the expression of ferrochelatase (FECH, an iron-sulfur cluster enzyme that inserts iron into protoporphyrin IX to form heme), is regulated by intracellular iron level. Iron 116-120 ferrochelatase Homo sapiens 67-71 34940556-4 2021 Moreover, it has been shown that the expression of ferrochelatase (FECH, an iron-sulfur cluster enzyme that inserts iron into protoporphyrin IX to form heme), is regulated by intracellular iron level. Iron 189-193 ferrochelatase Homo sapiens 51-65 34940556-4 2021 Moreover, it has been shown that the expression of ferrochelatase (FECH, an iron-sulfur cluster enzyme that inserts iron into protoporphyrin IX to form heme), is regulated by intracellular iron level. Iron 189-193 ferrochelatase Homo sapiens 67-71 34940556-8 2021 Finally, we will summarize what is known of FECH interactions with other proteins involved in iron metabolism in the mitochondria. Iron 94-98 ferrochelatase Homo sapiens 44-48 34582890-2 2021 The essential step of insertion of iron into the porphyrin macrocycle is mediated by the enzyme ferrochelatase. Iron 35-39 ferrochelatase Homo sapiens 96-110 8408820-1 1993 Erythropoietic protoporphyria is an inherited disorder characterized biochemically by a deficiency of ferrochelatase, the enzyme that catalyzes the incorporation of ferrous iron into protoporphyrin to form heme. Iron 165-177 ferrochelatase Homo sapiens 102-116 1343225-1 1992 The photodermatosis in erythropoietic protoporphyria (EPP) is caused by the accumulation of photosensitizing protoporphyrin (PP) in the skin, due to a defect in ferrochelatase, the enzyme that inserts ferrous iron into PP to form heme. Iron 201-213 ferrochelatase Homo sapiens 161-175 2189166-2 1990 The critical target seems to be the enzyme heme synthetase, which is essential for the insertion of iron into the precursor, protoporphyrin IX. Iron 100-104 ferrochelatase Homo sapiens 43-58 35309058-8 2022 The mechanisms involved in the iron uptake downregulation in EPP remain unclear, and the role of PPIX accumulation in microcytosis. Iron 31-35 ferrochelatase Homo sapiens 61-64 3327439-3 1987 A variety of biochemical and clinical evidence viewed in toto now suggests that ferrochelatase catalyzes zinc protoporphyrin formation in states of relative iron-deficient erythropoiesis and in lead-inhibited iron metabolism. Iron 157-161 ferrochelatase Homo sapiens 80-94 35054318-2 2022 The ubiquitous FECH catalyzes the insertion of iron into the protoporphyrin ring to generate the final product, heme. Iron 47-51 ferrochelatase Homo sapiens 15-19 3445653-3 1987 Since, as a rule, there is no iron deficit in haemodialysis, a secondary damage of the ferrochelatase, which physiologically by administration of iron leads to haem (ferroprotoporphyrin), is assumed as cause of the increase of erythrocytic protoporphyrin. Iron 146-150 ferrochelatase Homo sapiens 87-101 7252240-4 1981 The activity of heme synthease (ferrochelatase), which catalyzes the chelation of ferrous iron to protoporphyrin, is deficient in tissues of patients with protoporphyria. Iron 90-94 ferrochelatase Homo sapiens 32-46 4063392-6 1985 The availability of the mitochondrial iron pool for heme synthesis by mitochondria in vitro was studied using a recently developed HPLC method for the assay of ferrochelatase activity. Iron 38-42 ferrochelatase Homo sapiens 160-174 4063392-12 1985 The possibility that the mitochondrial iron pool functions as the proximate iron donor for heme synthesis by ferrochelatase in vivo is discussed. Iron 39-43 ferrochelatase Homo sapiens 109-123 4063392-12 1985 The possibility that the mitochondrial iron pool functions as the proximate iron donor for heme synthesis by ferrochelatase in vivo is discussed. Iron 76-80 ferrochelatase Homo sapiens 109-123 6425295-8 1984 The affinity of the enzyme for zinc lowers the actual determination of ferrochelatase activity with iron as substrate. Iron 100-104 ferrochelatase Homo sapiens 71-85 6639671-5 1983 We investigated the mechanistic basis for such acute reduction and report that iron was not only required as a co-substrate for I-P-450 heme formation, but also as a regulator of two key heme-synthetic enzymes, delta-aminolevulinic acid synthetase and ferrochelatase. Iron 79-83 ferrochelatase Homo sapiens 252-266 440897-1 1979 A 5-month-old infant with hypochromic anemia and iron overload secondary to ferrochelatase (heme synthetase) deficiency is described. Iron 49-53 ferrochelatase Homo sapiens 76-90 6243966-11 1980 Although the biological significance of this iron pool is not yet clear, it is likely that it represents a transit iron pool being the proximate iron donor for heme synthesis catalyzed by the enzyme ferrochelatase. Iron 45-49 ferrochelatase Homo sapiens 199-213 6243966-11 1980 Although the biological significance of this iron pool is not yet clear, it is likely that it represents a transit iron pool being the proximate iron donor for heme synthesis catalyzed by the enzyme ferrochelatase. Iron 115-119 ferrochelatase Homo sapiens 199-213 6243966-11 1980 Although the biological significance of this iron pool is not yet clear, it is likely that it represents a transit iron pool being the proximate iron donor for heme synthesis catalyzed by the enzyme ferrochelatase. Iron 115-119 ferrochelatase Homo sapiens 199-213 7356682-1 1980 Heme synthase (ferrochelatase) activity, as determined by the chelation of ferrous iron to protoporphyrin or deuteroporphyrin, is reduced to 10-25% of normal in tissues of patients with protoporphyria. Iron 75-87 ferrochelatase Homo sapiens 0-13 7356682-1 1980 Heme synthase (ferrochelatase) activity, as determined by the chelation of ferrous iron to protoporphyrin or deuteroporphyrin, is reduced to 10-25% of normal in tissues of patients with protoporphyria. Iron 75-87 ferrochelatase Homo sapiens 15-29 915001-1 1977 The activity of heme synthetase, which catalyzes the chelation of ferrous iron to protoporphyrin to form heme, is deficient in sonicates of skin fibroblasts cultured from patients with protoporphyria. Iron 66-78 ferrochelatase Homo sapiens 16-31 4234495-0 1968 [Effect of adenine nucleotides and iron on the heme-synthetase activity "in vitro"]. Iron 35-39 ferrochelatase Homo sapiens 47-62 1184741-2 1975 The final step in heme biosynthesis is chelation of porphyrin with Fe++ catalyzed by the mitochondrial enzyme heme synthetase. Iron 67-71 ferrochelatase Homo sapiens 110-125 810795-4 1975 These flagellates, in the presence of protoporphyrin IX, incorporated 59Fe into heme, indicating that they possess ferrochelatase (EC 4.99.1.1), the terminal enzyme in the heme biosynthetic pathway, which catalyzes the insertion of iron into protoporphyrin IX. Iron 232-236 ferrochelatase Homo sapiens 115-129 810795-4 1975 These flagellates, in the presence of protoporphyrin IX, incorporated 59Fe into heme, indicating that they possess ferrochelatase (EC 4.99.1.1), the terminal enzyme in the heme biosynthetic pathway, which catalyzes the insertion of iron into protoporphyrin IX. Iron 232-236 ferrochelatase Homo sapiens 131-142 5431821-0 1970 [Effect of the concentration of iron and pyridoxal phosphate on the ferrochelatase activity of erythrocytes]. Iron 32-36 ferrochelatase Homo sapiens 68-82 7354807-3 1980 We measured the activities of protoporphyrinogen oxidase, which catalyzes the oxidation of protoporphyrinogen to protoporphyrin, and heme synthase, which catalyzes the chelation of iron to protoporphyrins, in cultured skin fibroblasts from five normal controls and five patients with variegate porphyria. Iron 181-185 ferrochelatase Homo sapiens 133-146 33475175-2 2021 FECH catalyzes the chelation of iron into protoporphyrin IX to form heme. Iron 32-36 ferrochelatase Homo sapiens 0-4 30767226-2 2019 The iron chelator deferoxamine (DFO) has been widely used to enhance PpIX accumulation by inhibiting the iron-dependent bioconversion of PpIX to heme, a reaction catalyzed by ferrochelatase (FECH). Iron 105-109 ferrochelatase Homo sapiens 175-189 31076252-7 2019 In this study, we demonstrated that iron deprivation increased the amount of ALAS2 mRNA as well as the ratio of ALAS2 to FECH mRNAs in cultured erythroleukemic K562 cells. Iron 36-40 ferrochelatase Homo sapiens 121-125 30767226-2 2019 The iron chelator deferoxamine (DFO) has been widely used to enhance PpIX accumulation by inhibiting the iron-dependent bioconversion of PpIX to heme, a reaction catalyzed by ferrochelatase (FECH). Iron 4-8 ferrochelatase Homo sapiens 175-189 30767226-2 2019 The iron chelator deferoxamine (DFO) has been widely used to enhance PpIX accumulation by inhibiting the iron-dependent bioconversion of PpIX to heme, a reaction catalyzed by ferrochelatase (FECH). Iron 105-109 ferrochelatase Homo sapiens 191-195 30767226-2 2019 The iron chelator deferoxamine (DFO) has been widely used to enhance PpIX accumulation by inhibiting the iron-dependent bioconversion of PpIX to heme, a reaction catalyzed by ferrochelatase (FECH). Iron 4-8 ferrochelatase Homo sapiens 191-195 28185024-1 2017 Patients with erythropoietic protoporphyria (EPP) have reduced activity of the enzyme ferrochelatase that catalyzes the insertion of iron into protoporphyrin IX (PPIX) to form heme. Iron 133-137 ferrochelatase Homo sapiens 86-100 30517741-6 2019 In addition, the PIH-mediated downregulation of human FECH is associated with iron chelation. Iron 78-82 ferrochelatase Homo sapiens 54-58 29247132-0 2017 The heme synthesis defect of mutants impaired in mitochondrial iron-sulfur protein biogenesis is caused by reversible inhibition of ferrochelatase. Iron 63-67 ferrochelatase Homo sapiens 132-146 24864106-4 2014 The biogenesis of [Fe-S] centers is crucial for heme synthesis because these co-factors determine the activity of IRP1 and that of ferrochelatase, an enzyme responsible for the insertion of an iron into protoporphyrin IX to produce heme. Iron 193-197 ferrochelatase Homo sapiens 131-145 26100117-5 2016 We observed that the K101Q mutation (due to c. 301 A>C mutation) may prevent the binding of [Fe-S] to GLRX5 protein, while L148S (due to c. 443 T>C mutation) may interfere with [Fe-S] transfer from GLRX5 to iron regulatory protein 1 (IRP1), mitochondrial aconitase (m-aconitase) and ferrochelatase. Iron 96-100 ferrochelatase Homo sapiens 272-303 25826316-3 2015 In this study, we investigated the iron-dependent process of heme maturation in Bacillus subtilis and present, for the first time, structural evidence for the physical interaction of a frataxin homologue (Fra), which is suggested to act as a regulatory component as well as an iron chaperone in different cellular pathways, and a ferrochelatase (HemH), which catalyses the final step of heme b biogenesis. Iron 35-39 ferrochelatase Homo sapiens 330-344 25826316-5 2015 Hydrogen-deuterium exchange experiments identified the landscape of the Fra/HemH interaction interface and revealed Fra as a specific ferrous iron donor for the ferrochelatase HemH. Iron 142-146 ferrochelatase Homo sapiens 161-175 27801584-0 2016 Human Ferrochelatase: Insights for the Mechanism of Ferrous Iron Approaching Protoporphyrin IX by QM/MM and QTCP Free Energy Studies. Iron 60-64 ferrochelatase Homo sapiens 6-20 27801584-1 2016 Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX, the terminal step in heme biosynthesis. Iron 42-54 ferrochelatase Homo sapiens 0-14 27627839-1 2016 In erythroid cells, more than 90% of transferrin-derived iron enters mitochondria where ferrochelatase inserts Fe2+ into protoporphyrin IX. Iron 57-61 ferrochelatase Homo sapiens 88-102 27627839-2 2016 However, the path of iron from endosomes to mitochondrial ferrochelatase remains elusive. Iron 21-25 ferrochelatase Homo sapiens 58-72 27627839-4 2016 In contrast, this study supports the hypothesis that the highly efficient transport of iron toward ferrochelatase in erythroid cells requires a direct interaction between transferrin-endosomes and mitochondria (the "kiss-and-run" hypothesis). Iron 87-91 ferrochelatase Homo sapiens 99-113 25179834-2 2015 Ferrochelatase (FECH), the last enzyme of this pathway, inserts iron into protoporphyrin IX (PPIX) to form heme. Iron 64-68 ferrochelatase Homo sapiens 0-14 25179834-2 2015 Ferrochelatase (FECH), the last enzyme of this pathway, inserts iron into protoporphyrin IX (PPIX) to form heme. Iron 64-68 ferrochelatase Homo sapiens 16-20 23787363-0 2013 Iron availability modulates aberrant splicing of ferrochelatase through the iron- and 2-oxoglutarate dependent dioxygenase Jmjd6 and U2AF(65.). Iron 0-4 ferrochelatase Homo sapiens 49-63 23787363-0 2013 Iron availability modulates aberrant splicing of ferrochelatase through the iron- and 2-oxoglutarate dependent dioxygenase Jmjd6 and U2AF(65.). Iron 76-80 ferrochelatase Homo sapiens 49-63 23787363-5 2013 Our study demonstrated that under iron deficient conditions, the aberrant splice product was increased to 56% and 50% of total FECH mRNA in erythroleukemic K562 and lymphoblastoid cell lines, respectively, both being homozygous for IVS3-48T. Iron 34-38 ferrochelatase Homo sapiens 127-131 22862424-3 2013 The bacterial expression of human frataxin stimulated maturation of human ferrochelatase, which catalyzes the insertion of iron into protoporphyrin at the last step of heme biosynthesis. Iron 123-127 ferrochelatase Homo sapiens 74-88 22897320-1 2012 Human ferrochelatase (EC 4.99.1.1) catalyzes the insertion ferrous iron into protoporphyrin IX as the last step in heme biosynthesis, an essential process to most organisms given the vast intracellular functions of heme. Iron 67-71 ferrochelatase Homo sapiens 6-20 22897320-1 2012 Human ferrochelatase (EC 4.99.1.1) catalyzes the insertion ferrous iron into protoporphyrin IX as the last step in heme biosynthesis, an essential process to most organisms given the vast intracellular functions of heme. Iron 67-71 ferrochelatase Homo sapiens 22-33 22897320-2 2012 Even with multiple ferrochelatase structures available, the exact mechanism for iron insertion into porphyrin is still a matter for debate. Iron 80-84 ferrochelatase Homo sapiens 19-33 22897320-10 2012 These results provide a rigorous view of the ferrochelatase mechanism through the inclusion of dynamic information, reveal new structural areas for functional investigation, and offer new insight into a potential iron channel to the active site. Iron 213-217 ferrochelatase Homo sapiens 45-59 22020364-6 2011 In addition, our results show that MCF-7/DOX cells are capable of producing higher levels of porphyrins than MCF-7/WT cells due to low expression of the enzyme ferrochelatase, which inserts iron into the tetra-pyrrol ring to form the end product heme. Iron 190-194 ferrochelatase Homo sapiens 160-174 22712763-1 2012 Ferrochelatase catalyzes the formation of protoheme from two potentially cytotoxic products, iron and protoporphyrin IX. Iron 93-97 ferrochelatase Homo sapiens 0-14 21627978-3 2011 The major focus was mitoferrin-1 (MFRN1), the mitochondrial transporter of Fe used for heme formation by FECH and for 2Fe2S cluster synthesis, which is critical to FECH activity/stability. Iron 75-77 ferrochelatase Homo sapiens 105-109 21627978-3 2011 The major focus was mitoferrin-1 (MFRN1), the mitochondrial transporter of Fe used for heme formation by FECH and for 2Fe2S cluster synthesis, which is critical to FECH activity/stability. Iron 75-77 ferrochelatase Homo sapiens 164-168 20427704-4 2010 Fech is the terminal heme synthesis enzyme to catalyze the insertion of the imported iron into protoporphyrin IX to produce heme. Iron 85-89 ferrochelatase Homo sapiens 0-4 21776189-1 2011 Ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous iron into protoporphyrin IX to give heme. Iron 97-109 ferrochelatase Homo sapiens 0-14 21852895-1 2011 Ferrochelatase (also known as PPIX ferrochelatase; Enzyme Commission number 4.9.9.1.1) catalyzes the insertion of ferrous iron into PPIX to form heme. Iron 114-126 ferrochelatase Homo sapiens 35-49 21852895-5 2011 It is generally believed that ferrous iron is directly channeled to ferrochelatase in vivo, but the identity of the suspected chaperone remains uncertain despite much recent progress in this area. Iron 38-42 ferrochelatase Homo sapiens 68-82 21852895-0 2011 FERROCHELATASE: THE CONVERGENCE OF THE PORPHYRIN BIOSYNTHESIS AND IRON TRANSPORT PATHWAYS. Iron 66-70 ferrochelatase Homo sapiens 0-14 21852895-1 2011 Ferrochelatase (also known as PPIX ferrochelatase; Enzyme Commission number 4.9.9.1.1) catalyzes the insertion of ferrous iron into PPIX to form heme. Iron 114-126 ferrochelatase Homo sapiens 0-14 20427704-7 2010 Our findings imply that Fech forms an oligomeric complex with Mfrn1 and Abcb10 to synergistically integrate mitochondrial iron importation and use for heme biosynthesis. Iron 122-126 ferrochelatase Homo sapiens 24-28 20622448-0 2010 Porcine ferrochelatase: the relationship between iron-removal reaction and the conversion of heme to Zn-protoporphyrin. Iron 49-53 ferrochelatase Homo sapiens 8-22 19965627-0 2010 Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery. Iron 91-95 ferrochelatase Homo sapiens 60-74 19965627-0 2010 Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery. Iron 120-124 ferrochelatase Homo sapiens 60-74 19965627-1 2010 Mammalian ferrochelatase, the terminal enzyme in the heme biosynthetic pathway, possesses an iron-sulfur [2Fe-2S] cluster that does not participate in catalysis. Iron 93-97 ferrochelatase Homo sapiens 10-24 19965627-6 2010 Ferrochelatase was also severely depleted in muscle biopsies and cultured myoblasts from patients with ISCU myopathy, a disease caused by deficiency of a scaffold protein required for Fe-S cluster assembly. Iron 184-188 ferrochelatase Homo sapiens 0-14 19965627-7 2010 Together, these data suggest that decreased Fe-S cluster availability because of cellular iron depletion or impaired Fe-S cluster assembly causes reduced maturation and stabilization of apo-ferrochelatase, providing a direct link between Fe-S biogenesis and completion of heme biosynthesis. Iron 44-48 ferrochelatase Homo sapiens 190-204 19965627-7 2010 Together, these data suggest that decreased Fe-S cluster availability because of cellular iron depletion or impaired Fe-S cluster assembly causes reduced maturation and stabilization of apo-ferrochelatase, providing a direct link between Fe-S biogenesis and completion of heme biosynthesis. Iron 90-94 ferrochelatase Homo sapiens 190-204 19965627-7 2010 Together, these data suggest that decreased Fe-S cluster availability because of cellular iron depletion or impaired Fe-S cluster assembly causes reduced maturation and stabilization of apo-ferrochelatase, providing a direct link between Fe-S biogenesis and completion of heme biosynthesis. Iron 117-121 ferrochelatase Homo sapiens 190-204 19965627-7 2010 Together, these data suggest that decreased Fe-S cluster availability because of cellular iron depletion or impaired Fe-S cluster assembly causes reduced maturation and stabilization of apo-ferrochelatase, providing a direct link between Fe-S biogenesis and completion of heme biosynthesis. Iron 117-121 ferrochelatase Homo sapiens 190-204 20622448-5 2010 To characterize the iron-removal reverse activity of FECH, we examined its properties in porcine liver and muscle mitochondria, and isolated porcine FECH cDNA. Iron 20-24 ferrochelatase Homo sapiens 53-57 16870250-2 2007 Moderately elevated free erythrocyte protoporphyrin (FEP) levels have been described in IASA, suggesting that the activity of ferrochelatase, the enzyme that catalyzes the final step in heme biosynthesis (incorporation of ferrous iron into protoporphyrin), might be diminished in erythroid progenitor cells from IASA patients. Iron 222-234 ferrochelatase Homo sapiens 126-140 19703464-4 2009 One unanswered question about ferrochelatase involves defining the mechanism whereby some metals, such as divalent Fe, Co, Ni, and Zn, can be used by the enzyme in vitro to produce the corresponding metalloporphyrins, while other metals, such as divalent Mn, Hg, Cd, or Pb, are inhibitors of the enzyme. Iron 115-117 ferrochelatase Homo sapiens 30-44 18044970-0 2007 Heme synthase (ferrochelatase) catalyzes the removal of iron from heme and demetalation of metalloporphyrins. Iron 56-60 ferrochelatase Homo sapiens 0-13 18044970-0 2007 Heme synthase (ferrochelatase) catalyzes the removal of iron from heme and demetalation of metalloporphyrins. Iron 56-60 ferrochelatase Homo sapiens 15-29 18044970-5 2007 Purification of the iron-removal enzyme showed that it was identical to ferrochelatase. Iron 20-24 ferrochelatase Homo sapiens 72-86 18044970-6 2007 Recombinant ferrochelatase in combination with NADH-cytochrome b5 reductase catalyzed NADH-dependent iron-removal reaction from hemin and hemoproteins. Iron 101-105 ferrochelatase Homo sapiens 12-26 17566985-1 2007 The final step in heme biosynthesis, insertion of ferrous iron into protoporphyrin IX, is catalyzed by protoporphyrin IX ferrochelatase (EC 4.99.1.1). Iron 50-62 ferrochelatase Homo sapiens 121-135 17566985-1 2007 The final step in heme biosynthesis, insertion of ferrous iron into protoporphyrin IX, is catalyzed by protoporphyrin IX ferrochelatase (EC 4.99.1.1). Iron 50-62 ferrochelatase Homo sapiens 137-148 17567154-2 2007 Ferrochelatase catalyzes the terminal step in heme biosynthesis, the insertion of ferrous iron into protoporphyrin to form protoheme IX. Iron 82-94 ferrochelatase Homo sapiens 0-14 17499976-3 2007 Iron-sulfur (Fe/S) clusters are required in two enzymes of heme biosynthesis in humans i.e. in ferrochelatase and adrenodoxin. Iron 13-15 ferrochelatase Homo sapiens 95-109 19767646-1 2009 Protoporphyrin IX ferrochelatase (EC 4.99.1.1) catalyzes the terminal step in the heme biosynthetic pathway, the insertion of ferrous iron into protoporphyrin IX. Iron 126-138 ferrochelatase Homo sapiens 18-32 19767646-1 2009 Protoporphyrin IX ferrochelatase (EC 4.99.1.1) catalyzes the terminal step in the heme biosynthetic pathway, the insertion of ferrous iron into protoporphyrin IX. Iron 126-138 ferrochelatase Homo sapiens 34-45 19955842-6 2009 In contrast, the ALA-mediated PpIX accumulation was increased by deferoxamine, an iron chelator, manganese and nitric oxide, which is contributed to PpIX metabolism by inhibiting ferrochelatase activity, generated by a nitric oxide-generating reagent NOC-18. Iron 82-86 ferrochelatase Homo sapiens 179-193 17884090-1 2007 Ferrochelatase (protoheme ferrolyase, EC 4.99.1.1) is the terminal enzyme in heme biosynthesis and catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX (heme). Iron 126-138 ferrochelatase Homo sapiens 0-14 17711525-1 2007 Erythropoietic protoporphyria (EPP) is an inherited disorder of haem biosynthesis caused by decreased activity of the enzyme ferrochelatase (FECH), which catalyses the insertion of iron into protoporphyrin, the last step in haem biosynthesis. Iron 181-185 ferrochelatase Homo sapiens 125-139 17711525-1 2007 Erythropoietic protoporphyria (EPP) is an inherited disorder of haem biosynthesis caused by decreased activity of the enzyme ferrochelatase (FECH), which catalyses the insertion of iron into protoporphyrin, the last step in haem biosynthesis. Iron 181-185 ferrochelatase Homo sapiens 141-145 17261801-1 2007 Ferrochelatase, the terminal enzyme in heme biosynthesis, catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX. Iron 93-97 ferrochelatase Homo sapiens 0-14 15312748-1 2004 Ferrochelatase (FECH), the last enzyme of the heme biosynthetic pathway, catalyzes the insertion of iron into protoporphyrin to form heme. Iron 100-104 ferrochelatase Homo sapiens 0-14 16614385-1 2006 Ferrochelatase (protohaem ferrolyase, EC 4.99.1.1), the terminal enzyme of the haem biosynthetic pathway, catalyses the insertion of ferrous iron into protoporphyrin IX to form protohaem. Iron 133-145 ferrochelatase Homo sapiens 0-14 16469498-4 2006 We evaluate the recently recognized interaction between ferrochelatase and frataxin as a way to regulate iron delivery to ferrochelatase, and thus iron and heme metabolism. Iron 105-109 ferrochelatase Homo sapiens 56-70 16469498-4 2006 We evaluate the recently recognized interaction between ferrochelatase and frataxin as a way to regulate iron delivery to ferrochelatase, and thus iron and heme metabolism. Iron 105-109 ferrochelatase Homo sapiens 122-136 16469498-4 2006 We evaluate the recently recognized interaction between ferrochelatase and frataxin as a way to regulate iron delivery to ferrochelatase, and thus iron and heme metabolism. Iron 147-151 ferrochelatase Homo sapiens 56-70 16469498-4 2006 We evaluate the recently recognized interaction between ferrochelatase and frataxin as a way to regulate iron delivery to ferrochelatase, and thus iron and heme metabolism. Iron 147-151 ferrochelatase Homo sapiens 122-136 17017521-2 2006 Frataxin participates in the synthesis of iron-sulfur clusters (ISCs), cofactors of several enzymes, including mitochondrial and cytosolic aconitase, complexes I, II and III of the respiratory chain, and ferrochelatase. Iron 42-46 ferrochelatase Homo sapiens 129-218 16839620-1 2006 Most iron in mammalian systems is routed to mitochondria to serve as a substrate for ferrochelatase. Iron 5-9 ferrochelatase Homo sapiens 85-99 16839620-2 2006 Ferrochelatase inserts iron into protoporphyrin IX to form heme which is incorporated into hemoglobin and cytochromes, the dominant hemoproteins in mammals. Iron 23-27 ferrochelatase Homo sapiens 0-14 15312748-1 2004 Ferrochelatase (FECH), the last enzyme of the heme biosynthetic pathway, catalyzes the insertion of iron into protoporphyrin to form heme. Iron 100-104 ferrochelatase Homo sapiens 16-20 15532727-1 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. Iron 80-92 ferrochelatase Homo sapiens 22-36 15532727-1 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. Iron 80-92 ferrochelatase Homo sapiens 38-49 12417755-1 2002 Heme, a major functional form of iron in the cell, is synthesized in the mitochondria by ferrochelatase inserting ferrous iron into protoporphyrin IX. Iron 33-37 ferrochelatase Homo sapiens 89-103 12782026-1 2003 A continuous spectrofluorimetric assay for determining ferrochelatase activity has been developed using the physiological substrates ferrous iron and protoporphyrin IX under strictly anaerobic conditions. Iron 141-145 ferrochelatase Homo sapiens 55-69 15123683-0 2004 Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis. Iron 18-22 ferrochelatase Homo sapiens 35-49 15123683-1 2004 Human ferrochelatase, a mitochondrial membrane-associated protein, catalyzes the terminal step of heme biosynthesis by insertion of ferrous iron into protoporphyrin IX. Iron 132-144 ferrochelatase Homo sapiens 6-65 15123683-2 2004 The recently solved x-ray structure of human ferrochelatase identifies a potential binding site for an iron donor protein on the matrix side of the homodimer. Iron 103-107 ferrochelatase Homo sapiens 45-59 15123683-3 2004 Herein we demonstrate Hs holofrataxin to be a high affinity iron binding partner for Hs ferrochelatase that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis. Iron 60-64 ferrochelatase Homo sapiens 88-102 15123683-3 2004 Herein we demonstrate Hs holofrataxin to be a high affinity iron binding partner for Hs ferrochelatase that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis. Iron 60-64 ferrochelatase Homo sapiens 146-160 15123683-3 2004 Herein we demonstrate Hs holofrataxin to be a high affinity iron binding partner for Hs ferrochelatase that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis. Iron 138-142 ferrochelatase Homo sapiens 88-102 15123683-3 2004 Herein we demonstrate Hs holofrataxin to be a high affinity iron binding partner for Hs ferrochelatase that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis. Iron 138-142 ferrochelatase Homo sapiens 146-160 15123683-5 2004 In essence, the distinct binding affinities of holofrataxin to the target proteins, ferrochelatase (heme synthesis) and ISU (iron-sulfur cluster synthesis), allows discrimination between the two major iron-dependent pathways and facilitates targeted heme biosynthesis following down-regulation of frataxin. Iron 201-205 ferrochelatase Homo sapiens 84-98 12417755-1 2002 Heme, a major functional form of iron in the cell, is synthesized in the mitochondria by ferrochelatase inserting ferrous iron into protoporphyrin IX. Iron 114-126 ferrochelatase Homo sapiens 89-103 11502175-0 2001 Human ferrochelatase: characterization of substrate-iron binding and proton-abstracting residues. Iron 52-56 ferrochelatase Homo sapiens 6-20 12196181-2 2002 In erythroid cells the vast majority of Fe released from endosomes must cross both the outer and the inner mitochondrial membranes to reach ferrochelatase, which inserts Fe into protoporphyrin IX. Iron 40-42 ferrochelatase Homo sapiens 140-154 12196181-2 2002 In erythroid cells the vast majority of Fe released from endosomes must cross both the outer and the inner mitochondrial membranes to reach ferrochelatase, which inserts Fe into protoporphyrin IX. Iron 170-172 ferrochelatase Homo sapiens 140-154 12196181-3 2002 Based on the fact that Fe is specifically targeted into erythroid mitochondria, we have proposed that a transient mitochondria-endosome interaction is involved in Fe transfer to ferrochelatase [Ponka (1997) Blood 89, 1-25]. Iron 23-25 ferrochelatase Homo sapiens 178-192 11502175-1 2001 The terminal step in heme biosynthesis, the insertion of ferrous iron into protoporphyrin IX to form protoheme, is catalyzed by the enzyme ferrochelatase (EC 4.99.1.1). Iron 57-69 ferrochelatase Homo sapiens 139-153 11502175-1 2001 The terminal step in heme biosynthesis, the insertion of ferrous iron into protoporphyrin IX to form protoheme, is catalyzed by the enzyme ferrochelatase (EC 4.99.1.1). Iron 57-69 ferrochelatase Homo sapiens 155-166 11039124-1 2000 UNLABELLED: Erythropoietic protoporphyria (EPP, MIM 177000) is an inherited disorder caused by a partial deficiency of ferrochelatase (FECH) which catalyses the chelation of iron into protoporphyrin to form haem. Iron 174-178 ferrochelatase Homo sapiens 135-139 11451377-6 2001 The soluble ferrochelatase contained one mole of iron in each mole of the enzyme. Iron 49-53 ferrochelatase Homo sapiens 12-26 10996833-2 2000 FMO is an intracellular ferrireductase which may be responsible for the obligatory reduction of ferric to ferrous iron so that reduced iron can be incorporated into heme by ferrochelatase. Iron 114-118 ferrochelatase Homo sapiens 173-187 10996833-2 2000 FMO is an intracellular ferrireductase which may be responsible for the obligatory reduction of ferric to ferrous iron so that reduced iron can be incorporated into heme by ferrochelatase. Iron 135-139 ferrochelatase Homo sapiens 173-187 10942404-0 2000 Mutations in the iron-sulfur cluster ligands of the human ferrochelatase lead to erythropoietic protoporphyria. Iron 17-21 ferrochelatase Homo sapiens 58-72 10942404-11 2000 The mutations of the codons for 2 of the [2Fe-2S] cluster ligands in patients with EPP supports the importance of the iron-sulfur center for the proper functioning of mammalian FECH and, in at least humans, its absence has a direct clinical impact. Iron 118-122 ferrochelatase Homo sapiens 177-181 10903501-0 2000 Regulation of the expression of human ferrochelatase by intracellular iron levels. Iron 70-74 ferrochelatase Homo sapiens 38-52 10903501-2 2000 To clarify the roles of the iron-sulfur cluster in the expression of mammalian ferrochelatase, enzyme activity in human erythroleukemia K562 cells under iron-depleted conditions was examined. Iron 28-32 ferrochelatase Homo sapiens 79-93 10903501-2 2000 To clarify the roles of the iron-sulfur cluster in the expression of mammalian ferrochelatase, enzyme activity in human erythroleukemia K562 cells under iron-depleted conditions was examined. Iron 153-157 ferrochelatase Homo sapiens 79-93 10903501-9 2000 When Escherichia coli ferrochelatase, which lacks the iron-sulfur cluster, was expressed in Cos7 cells, the activity did not change following any treatment. Iron 54-58 ferrochelatase Homo sapiens 22-36 10903501-11 2000 These results indicate that the expression of mammalian ferrochelatase is regulated by intracellular iron levels, via the iron-sulfur cluster center at the C-terminus, and this contributes to the regulation of the biosynthesis of heme at the terminal step. Iron 101-105 ferrochelatase Homo sapiens 56-70 10903501-11 2000 These results indicate that the expression of mammalian ferrochelatase is regulated by intracellular iron levels, via the iron-sulfur cluster center at the C-terminus, and this contributes to the regulation of the biosynthesis of heme at the terminal step. Iron 122-126 ferrochelatase Homo sapiens 56-70