A primer on heme biosynthesis

HA Dailey, AE Medlock - Biological Chemistry, 2022 - degruyter.com
Heme (protoheme IX) is an essential cofactor for a large variety of proteins whose functions
vary from one electron reactions to binding gases. While not ubiquitous, heme is found in the …

Diverse enzymatic chemistry for propionate side chain cleavages in tetrapyrrole biosynthesis

R Ushimaru, J Lyu, I Abe - Journal of Industrial Microbiology and …, 2023 - academic.oup.com
Tetrapyrroles represent a unique class of natural products that possess diverse chemical
architectures and exhibit a broad range of biological functions. Accordingly, they attract keen …

The Role of the Hydrogen Bond Network in Maintaining Heme Pocket Stability and Protein Function Specificity of C. diphtheriae Coproheme Decarboxylase

F Sebastiani, C Baroni, G Patil, A Dali, M Becucci… - Biomolecules, 2023 - mdpi.com
Monoderm bacteria accumulate heme b via the coproporphyrin-dependent biosynthesis
pathway. In the final step, in the presence of two molecules of H2O2, the propionate groups …

Exploiting differences in heme biosynthesis between bacterial species to screen for novel antimicrobials

LK Jackson, TA Dailey, B Anderle, MJ Warren… - Biomolecules, 2023 - mdpi.com
The final three steps of heme biogenesis exhibit notable differences between di-and mono-
derm bacteria. The former employs the protoporphyrin-dependent (PPD) pathway, while the …

Revisiting catalytic His and Glu residues in coproporphyrin ferrochelatase–unexpected activities of active site variants

T Gabler, A Dali, M Bellei, F Sebastiani… - The FEBS …, 2024 - Wiley Online Library
The identification of the coproporphyrin‐dependent heme biosynthetic pathway, which is
used almost exclusively by monoderm bacteria in 2015 by Dailey et al. triggered studies …

[HTML][HTML] An active site at work–the role of key Residues in C. Diphteriae Coproheme Decarboxylase

F Sebastiani, R Risorti, C Niccoli, H Michlits… - Journal of Inorganic …, 2022 - Elsevier
Coproheme decarboxylases (ChdCs) are utilized by monoderm bacteria to produce heme b
by a stepwise oxidative decarboxylation of the 2-and 4-propionate groups of iron …

Reorienting mechanism of harderoheme in coproheme decarboxylase—A computational study

W Liu, Y Pang, Y Song, X Li, H Tan, G Chen - International Journal of …, 2022 - mdpi.com
Coproheme decarboxylase (ChdC) is an important enzyme in the coproporphyrin-
dependent pathway (CPD) of Gram-positive bacteria that decarboxylates coproheme on two …

Insights into the flexibility of the domain‐linking loop in actinobacterial coproheme decarboxylase through structures and molecular dynamics simulations

G Patil, DJ Alonso de Armiño, Y Guo… - Protein …, 2025 - Wiley Online Library
Prokaryotic heme biosynthesis in Gram‐positive bacteria follows the coproporphyrin‐
dependent heme biosynthesis pathway. The last step in this pathway is catalyzed by the …

The role of the distal cavity in carbon monoxide stabilization in the coproheme decarboxylase enzyme from C. diphtheriae

F Sebastiani, A Dali, DJA de Armiño… - Journal of Inorganic …, 2023 - Elsevier
This work focuses on the carbon monoxide adducts of the wild-type and selected variants of
the coproheme decarboxylase from actinobacterial Corynebacterium diphtheriae complexed …

[HTML][HTML] Entrance channels to coproheme in coproporphyrin ferrochelatase probed by exogenous imidazole binding

A Dali, T Gabler, F Sebastiani, PG Furtmüller… - Journal of Inorganic …, 2024 - Elsevier
Iron insertion into porphyrins is an essential step in heme biosynthesis. In the
coproporphyrin-dependent pathway, specific to monoderm bacteria, this reaction is …