ArticleJournal of molecular biology2008
Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 62 citations in OpenAlex.
- Milestones in the Elucidation of Heme Biosynthesis.Chemical reviews · 2026Review
- Structural insights into the recognition of tetrapyrrole substrates by ancestral class II chelatase CfbA.Protein science : a publication of the Protein Society · 2024Article
- Iron insertion into coproporphyrin III-ferrochelatase complex: Evidence for an intermediate distorted catalytic species.Protein science : a publication of the Protein Society · 2023Article
- 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
- AI-driven pan-proteome analyses reveal insights into the biohydrometallurgical properties ofFrontiers in microbiology · 2023Article
- Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis.Computational and structural biotechnology journal · 2023Review
- Self-Assembly of Chiral Cyclohexanohemicucurbit[Molecules (Basel, Switzerland) · 2022Article
- Ferrochelatase: Mapping the Intersection of Iron and Porphyrin Metabolism in the Mitochondria.Frontiers in cell and developmental biology · 2022Review
- Self-Metalation of Porphyrins at the Solid-Gas Interface.Angewandte Chemie (International ed. in English) · 2021Article
- Article
- Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase.The FEBS journal · 2020Article
- The Red Color of Life Transformed - Synthetic Advances and Emerging Applications of Protoporphyrin IX in Chemical Biology.European journal of organic chemistry · 2020Review
- Emergence of Ferrichelatase Activity in a Siderophore-Binding Protein Supports an Iron Shuttle in Bacteria.ACS central science · 2020Article
- Biophysical and X-ray structural studies of the (GGGTT)3GGG G-quadruplex in complex with N-methyl mesoporphyrin IX.PloS one · 2020Article
- Article
- Molecular Engineering of Free-Base Porphyrins as Ligands-The N-H⋅⋅⋅X Binding Motif in Tetrapyrroles.Angewandte Chemie (International ed. in English) · 2019Review
- Emerging Applications of Porphyrins and Metalloporphyrins in Biomedicine and Diagnostic Magnetic Resonance Imaging.Biosensors · 2018Review
- Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Microbiology and molecular biology reviews : MMBR · 2017Review
- Synthesis, delivery and regulation of eukaryotic heme and Fe-S cluster cofactors.Archives of biochemistry and biophysics · 2016Review
- Investigation by MD simulation of the key residues related to substrate-binding and heme-release in human ferrochelatase.Journal of molecular modeling · 2013Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The specific insertion of a divalent metal ion into tetrapyrrole macrocycles is catalyzed by a group of enzymes called chelatases. Distortion of the tetrapyrrole has been proposed to be an important component of the mechanism of metallation. We present the structures of two different inhibitor complexes: (1) N-methylmesoporphyrin (N-MeMP) with the His183Ala variant of Bacillus subtilis ferrochelatase; (2) the wild-type form of the same enzyme with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride (dSDP). Analysis of the structures showed that only one N-MeMP isomer out of the eight possible was bound to the protein and it was different from the isomer that was earlier found to bind to the wild-type enzyme. A comparison of the distortion of this porphyrin with other porphyrin complexes of ferrochelatase and a catalytic antibody with ferrochelatase activity using normal-coordinate structural decomposition reveals that certain types of distortion are predominant in all these complexes. On the other hand, dSDP, which binds closer to the protein surface compared to N-MeMP, does not undergo any distortion upon binding to the protein, underscoring that the position of the porphyrin within the active site pocket is crucial for generating the distortion required for metal insertion. In addition, in contrast to the wild-type enzyme, Cu(2+)-soaking of the His183Ala variant complex did not show any traces of porphyrin metallation. Collectively, these results provide new insights into the role of the active site residues of ferrochelatase in controlling stereospecificity, distortion and metallation.
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