ArticleJournal of molecular biology2009
Product release rather than chelation determines metal specificity for ferrochelatase.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 56 citations in OpenAlex.
- Milestones in the Elucidation of Heme Biosynthesis.Chemical reviews · 2026Review
- Ferruginous hemeprotein HhuH facilitates the cadmium adsorption and chromium reduction inApplied and environmental microbiology · 2025Article
- Structural Insights into Mechanisms Underlying Mitochondrial and Bacterial Cytochrome c Synthases.Biomolecules · 2024Article
- Nickel-chelatase activity of SirB variants mimicking the His arrangement in the naturally occurring nickel-chelatase CfbA.FEBS open bio · 2024Article
- Impact of Phosphorylation at Various Sites on the Active Pocket of Human Ferrochelatase: Insights from Molecular Dynamics Simulations.International journal of molecular sciences · 2024Article
- Genetic adaptations of sea anemone to hydrothermal environment.Science advances · 2023Article
- Microbial Synthesis of HemeMolecules (Basel, Switzerland) · 2023Review
- Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis.Computational and structural biotechnology journal · 2023Review
- Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023Review
- Iron Metabolism in the Disorders of Heme Biosynthesis.Metabolites · 2022Review
- 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
- The active site of magnesium chelatase.Nature plants · 2020Article
- The mitochondrial heme metabolon: Insights into the complex(ity) of heme synthesis and distribution.Molecular genetics and metabolism · 2019Review
- Ferrochelatase π-helix: Implications from examining the role of the conserved π-helix glutamates in porphyrin metalation and product release.Archives of biochemistry and biophysics · 2018Article
- Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Microbiology and molecular biology reviews : MMBR · 2017Review
- A Novel Role for Progesterone Receptor Membrane Component 1 (PGRMC1): A Partner and Regulator of Ferrochelatase.Biochemistry · 2016Article
- Purification, crystallization, crystallographic analysis and phasing of the CRISPR-associated protein Csm2 from Thermotoga maritima.Acta crystallographica. Section F, Structural biology communications · 2015Article
- HemQ: An iron-coproporphyrin oxidative decarboxylase for protoheme synthesis in Firmicutes and Actinobacteria.Archives of biochemistry and biophysics · 2015Review
- The Escherichia coli small protein MntS and exporter MntP optimize the intracellular concentration of manganese.PLoS genetics · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Ferrochelatase (protoheme ferrolyase, E.C. 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). Within the past two years, X-ray crystallographic data obtained with human ferrochelatase have clearly shown that significant structural changes occur during catalysis that are predicted to facilitate metal insertion and product release. 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. Through the use of high-resolution X-ray crystallography along with characterization of metal species via their anomalous diffraction, the identity and position of Hg, Cd, Ni, or Mn in the center of enzyme-bound porphyrin macrocycle were determined. When Pb, Hg, Cd, or Ni was present in the macrocycle, the conserved pi helix was in the extended, partially unwound "product release" state. Interestingly, in the structure of ferrochelatase with Mn-porphyrin bound, the pi helix is not extended or unwound and is in the "substrate-bound" conformation. These findings show that at least in the cases of Mn, Pb, Cd, and Hg, metal "inhibition" of ferrochelatase is not due to the inability of the enzyme to insert the metal into the macrocycle or by binding to a second metal binding site as has been previously proposed. Rather, inhibition occurs after metal insertion and results from poor or diminished product release. Possible explanations for the lack of product release are proposed herein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.