ArticleThe FEBS journal2020
Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase.
Article in The FEBS journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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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.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Milestones in the Elucidation of Heme Biosynthesis.Chemical reviews · 2026Review
- Heme in Bacterial Pathogenesis and as an Antimicrobial Target.Chemical reviews · 2025Review
- Structural insights into the recognition of tetrapyrrole substrates by ancestral class II chelatase CfbA.Protein science : a publication of the Protein Society · 2024Article
- The Molecular Evolution, Structure, and Function of Coproporphyrinogen Oxidase and Protoporphyrinogen Oxidase in Prokaryotes.Biology · 2023Article
- Iron insertion into coproporphyrin III-ferrochelatase complex: Evidence for an intermediate distorted catalytic species.Protein science : a publication of the Protein Society · 2023Article
- Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis.Computational and structural biotechnology journal · 2023Review
- Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin III: Propionate interactions and porphyrin core deformation.Protein science : a publication of the Protein Society · 2023Article
- Cryptic specialized metabolites driveProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Reorienting Mechanism of Harderoheme in Coproheme Decarboxylase-A Computational Study.International journal of molecular sciences · 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
- Understanding molecular enzymology of porphyrin-binding α + β barrel proteins - One fold, multiple functions.Biochimica et biophysica acta. Proteins and proteomics · 2021Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Coproporphyrin ferrochelatases (CpfCs, EC 4.99.1.9) insert ferrous iron into coproporphyrin III yielding coproheme. CpfCs are utilized by prokaryotic, mainly monoderm (Gram-positive) bacteria within the recently detected coproporphyrin-dependent (CPD) heme biosynthesis pathway. Here, we present a comprehensive study on CpfC from Listeria monocytogenes (LmCpfC) including the first crystal structure of a coproheme-bound CpfC. Comparison of crystal structures of apo-LmCpfC and coproheme-LmCpfC allowed identification of structural rearrangements and of amino acids involved in tetrapyrrole macrocycle and Fe
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Registered trials
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