ArticleThe Journal of biological chemistry2008
Metal ion substrate inhibition of ferrochelatase.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 48 citations in OpenAlex.
- Zinc Protoporphyrin IX in Meat and Meat Products: Formation, Application, and Future Perspectives.Food science of animal resources · 2025Review
- On the Possibility of Using 5-Aminolevulinic Acid in the Light-Induced Destruction of Microorganisms.International journal of molecular sciences · 2024Review
- Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis.Computational and structural biotechnology journal · 2023Review
- Insight into the function of active site residues in the catalytic mechanism of human ferrochelatase.The Biochemical journal · 2021Article
- The Small Protein CydX Is Required for CytochromeJournal of bacteriology · 2020Article
- Splitting the functions of Rim2, a mitochondrial iron/pyrimidine carrier.Mitochondrion · 2019Article
- The function of PROTOPORPHYRINOGEN IX OXIDASE in chlorophyll biosynthesis requires oxidised plastoquinone inCommunications biology · 2019Article
- 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
- A physiological perspective on the origin and evolution of photosynthesis.FEMS microbiology reviews · 2018Review
- Article
- The Structure of the Complex between Yeast Frataxin and Ferrochelatase: CHARACTERIZATION AND PRE-STEADY STATE REACTION OF FERROUS IRON DELIVERY AND HEME SYNTHESIS.The Journal of biological chemistry · 2016Article
- Refolding and enzyme kinetic studies on the ferrochelatase of the cyanobacterium Synechocystis sp. PCC 6803.PloS one · 2013Article
- Identification and characterization of solvent-filled channels in human ferrochelatase.Biochemistry · 2012Article
- Nickel(II) chelatase variants directly evolved from murine ferrochelatase: porphyrin distortion and kinetic mechanism.Biochemistry · 2011Article
- Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
- Silver nanoparticles embedded in zeolite membranes: release of silver ions and mechanism of antibacterial action.International journal of nanomedicine · 2011Article
- FERROCHELATASE: THE CONVERGENCE OF THE PORPHYRIN BIOSYNTHESIS AND IRON TRANSPORT PATHWAYS.Journal of porphyrins and phthalocyanines · 2011Article
- Identification and characterization of an inhibitory metal ion-binding site in ferrochelatase.The Journal of biological chemistry · 2010Article
- Structure and function of enzymes in heme biosynthesis.Protein science : a publication of the Protein Society · 2010Review
- Metal ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX to form heme. Robust kinetic analyses of the reaction mechanism are complicated by the instability of ferrous iron in aqueous solution, particularly at alkaline pH values. At pH 7.00 the half-life for spontaneous oxidation of ferrous ion is approximately 2 min in the absence of metal complexing additives, which is sufficient for direct comparisons of alternative metal ion substrates with iron. These analyses reveal that purified recombinant ferrochelatase from both murine and yeast sources inserts not only ferrous iron but also divalent cobalt, zinc, nickel, and copper into protoporphyrin IX to form the corresponding metalloporphyrins but with considerable mechanistic variability. Ferrous iron is the preferred metal ion substrate in terms of apparent k(cat) and is also the only metal ion substrate not subject to severe substrate inhibition. Substrate inhibition occurs in the order Cu(2+) > Zn(2+) > Co(2+) > Ni(2+) and can be alleviated by the addition of metal complexing agents such as beta-mercaptoethanol or imidazole to the reaction buffer. These data indicate the presence of two catalytically significant metal ion binding sites that may coordinately regulate a selective processivity for the various potential metal ion substrates.
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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.