ArticleBlood2005
Production and characterization of erythropoietic protoporphyric heterodimeric ferrochelatases.
Article in Blood, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 31 citations in OpenAlex.
- New Avenues of Heme Synthesis Regulation.International journal of molecular sciences · 2022Review
- Small-molecule inhibitors of ferrochelatase are antiangiogenic agents.Cell chemical biology · 2022Article
- Ferrochelatase: Mapping the Intersection of Iron and Porphyrin Metabolism in the Mitochondria.Frontiers in cell and developmental biology · 2022Review
- Insight into the function of active site residues in the catalytic mechanism of human ferrochelatase.The Biochemical journal · 2021Article
- Article
- A Novel Role for Progesterone Receptor Membrane Component 1 (PGRMC1): A Partner and Regulator of Ferrochelatase.Biochemistry · 2016Article
- Identification and characterization of solvent-filled channels in human ferrochelatase.Biochemistry · 2012Article
- Discovery and Characterization of HemQ: an essential heme biosynthetic pathway component.The Journal of biological chemistry · 2010Article
- Metal ion substrate inhibition of ferrochelatase.The Journal of biological chemistry · 2008Article
- A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase.Journal of molecular biology · 2007Article
- Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis.Biochemistry · 2007Article
- Contribution of a common single-nucleotide polymorphism to the genetic predisposition for erythropoietic protoporphyria.American journal of human genetics · 2006Article
- Production and characterization of erythropoietic protoporphyric heterodimeric ferrochelatases.Blood · 2005Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Mutations resulting in diminished activity of the dimeric enzyme ferrochelatase are a prerequisite for the inherited disorder erythropoietic protoporphyria (EPP). Patients with clinical EPP have only 10% to 30% of normal levels of ferrochelatase activity, and although many patients with EPP have one mutant allele and one "low-expression" normal allele, the possibility remains that, for some, low ferrochelatase activity may result from an EPP mutation that has an impact on both subunits of the wild-type/mutant heterodimer. Here we present data for 12 ferrochelatase wild-type/EPP mutant heterodimers showing that some mutations result in heterodimers with the residual activity anticipated from individual constituents, whereas others result in heterodimers with significantly lower activity than would be predicted. Although the data do not allow an a priori prediction of heterodimeric residual activity based solely on the in vitro activity of EPP homodimers or the position of the mutated residue within ferrochelatase, mutations that affect the dimer interface or [2Fe-2S] cluster have a significantly greater impact on residual activity than would be predicted. These data suggest that some EPP mutations may result in clinically overt EPP in the absence of a low-expression, wild-type allele; this is of potential significance for genetic counseling of patients with EPP.
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Registered trials
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