ArticleBiochemistry2018
Insights into the Active Site of Coproheme Decarboxylase from Listeria monocytogenes.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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Who cites it
17 citing papers in PubMed, 32 citations in OpenAlex.
- The role of conserved elements in an active site α-helix of coproheme decarboxylase.Journal of inorganic biochemistry · 2026Article
- Deciphering the role of the distal pocket in Staphylococcus aureus coproheme decarboxylase.Journal of inorganic biochemistry · 2025Article
- Insights into the flexibility of the domain-linking loop in actinobacterial coproheme decarboxylase through structures and molecular dynamics simulations.Protein science : a publication of the Protein Society · 2025Article
- Reactivity of Coproheme Decarboxylase with Monovinyl, Monopropionate Deuteroheme.Biomolecules · 2023Article
- Production of copropophyrin III, biliverdin and bilirubin by the rufomycin producer,Frontiers in microbiology · 2023Article
- Spectroscopic evidence of the effect of hydrogen peroxide excess on the coproheme decarboxylase from actinobacterialJournal of Raman spectroscopy : JRS · 2022Article
- Reorienting Mechanism of Harderoheme in Coproheme Decarboxylase-A Computational Study.International journal of molecular sciences · 2022Article
- Reaction intermediate rotation during the decarboxylation of coproheme to heme b in C. diphtheriae.Biophysical journal · 2021Article
- Investigating the Roles of Listeria monocytogenes Peroxidases in Growth and Virulence.Microbiology spectrum · 2021Article
- Article
- Understanding molecular enzymology of porphyrin-binding α + β barrel proteins - One fold, multiple functions.Biochimica et biophysica acta. Proteins and proteomics · 2021Review
- Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase.The FEBS journal · 2020Article
- Actinobacterial Coproheme Decarboxylases Use Histidine as a Distal Base to Promote Compound I Formation.ACS catalysis · 2020Article
- Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to HemeACS catalysis · 2019Article
- The hydrogen bonding network of coproheme in coproheme decarboxylase from Listeria monocytogenes: Effect on structure and catalysis.Journal of inorganic biochemistry · 2019Article
- Lysine as a heme iron ligand: A property common to three truncated hemoglobins from Chlamydomonas reinhardtii.Biochimica et biophysica acta. General subjects · 2018Article
- Formation and Cleavage of C-C Bonds by Enzymatic Oxidation-Reduction Reactions.Chemical reviews · 2018Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Coproheme decarboxylases (ChdC) catalyze the hydrogen peroxide-mediated conversion of coproheme to heme b. This work compares the structure and function of wild-type (WT) coproheme decarboxylase from Listeria monocytogenes and its M149A, Q187A, and M149A/Q187A mutants. The UV-vis, resonance Raman, and electron paramagnetic resonance spectroscopies clearly show that the ferric form of the WT protein is a pentacoordinate quantum mechanically mixed-spin state, which is very unusual in biological systems. Exchange of the Met149 residue to Ala dramatically alters the heme coordination, which becomes a 6-coordinate low spin species with the amide nitrogen atom of the Q187 residue bound to the heme iron. The interaction between M149 and propionyl 2 is found to play an important role in keeping the Q187 residue correctly positioned for closure of the distal cavity. This is confirmed by the observation that in the M149A variant two CO conformers are present corresponding to open (A
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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.