ArticleBiophysical journal2021
Reaction intermediate rotation during the decarboxylation of coproheme to heme b in C. diphtheriae.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 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
- Exploiting Differences in Heme Biosynthesis between Bacterial Species to Screen for Novel Antimicrobials.Biomolecules · 2023Article
- Reactivity of Coproheme Decarboxylase with Monovinyl, Monopropionate Deuteroheme.Biomolecules · 2023Article
- The Role of the Hydrogen Bond Network in Maintaining Heme Pocket Stability and Protein Function Specificity ofBiomolecules · 2023Article
- Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis.Computational and structural biotechnology journal · 2023Review
- 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
- Initial Steps to Engineer Coproheme Decarboxylase to Obtain Stereospecific Monovinyl, Monopropionyl Deuterohemes.Frontiers in bioengineering and biotechnology · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Monoderm bacteria utilize coproheme decarboxylases (ChdCs) to generate heme b by a stepwise decarboxylation of two propionate groups of iron coproporphyrin III (coproheme), forming two vinyl groups. This work focuses on actinobacterial ChdC from Corynebacterium diphtheriae (CdChdC) to elucidate the hydrogen peroxide-mediated decarboxylation of coproheme via monovinyl monopropionyl deuteroheme (MMD) to heme b, with the principal aim being to understand the reorientation mechanism of MMD during turnover. Wild-type CdChdC and variants, namely H118A, H118F, and A207E, were studied by resonance Raman and ultraviolet-visible spectroscopy, mass spectrometry, and molecular dynamics simulations. As actinobacterial ChdCs use a histidine (H118) as a distal base, we studied the H118A and H118F variants to elucidate the effect of 1) the elimination of the proton acceptor and 2) steric constraints within the active site. The A207E variant mimics the proximal H-bonding network found in chlorite dismutases. This mutation potentially increases the rigidity of the proximal site and might impair the rotation of the reaction intermediate MMD. We found that both wild-type CdChdC and the variant H118A convert coproheme mainly to heme b upon titration with H
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