Prokaryotic heme biosynthesis: multiple pathways to a common essential product

HA Dailey, TA Dailey, S Gerdes, D Jahn… - Microbiology and …, 2017 - Am Soc Microbiol
The advent of heme during evolution allowed organisms possessing this compound to
safely and efficiently carry out a variety of chemical reactions that otherwise were difficult or …

Heme synthesis and acquisition in bacterial pathogens

JE Choby, EP Skaar - Journal of molecular biology, 2016 - Elsevier
Bacterial pathogens require the iron-containing cofactor heme to cause disease. Heme is
essential to the function of hemoproteins, which are involved in energy generation by the …

Formation and cleavage of C–C bonds by enzymatic oxidation–reduction reactions

FP Guengerich, FK Yoshimoto - Chemical Reviews, 2018 - ACS Publications
Many oxidation–reduction (redox) enzymes, particularly oxygenases, have roles in reactions
that make and break C–C bonds. The list includes cytochrome P450 and other heme-based …

[HTML][HTML] Heme biosynthesis in prokaryotes

G Layer - Biochimica et Biophysica Acta (BBA)-Molecular Cell …, 2021 - Elsevier
The cyclic tetrapyrrole heme is used as a prosthetic group in a broad variety of different
proteins in almost all organisms. Often, it is essential for vital biochemical processes such as …

[HTML][HTML] Understanding molecular enzymology of porphyrin-binding α+ β barrel proteins-One fold, multiple functions

S Hofbauer, V Pfanzagl, H Michlits, D Schmidt… - … et Biophysica Acta (BBA …, 2021 - Elsevier
There is a high functional diversity within the structural superfamily of porphyrin-binding
dimeric α+ β barrel proteins. In this review we aim to analyze structural constraints of chlorite …

Structure-based mechanism for oxidative decarboxylation reactions mediated by amino acids and heme propionates in coproheme decarboxylase (HemQ)

AI Celis, GH Gauss, BR Streit, K Shisler… - Journal of the …, 2017 - ACS Publications
Coproheme decarboxylase catalyzes two sequential oxidative decarboxylations with H2O2
as the oxidant, coproheme III as substrate and cofactor, and heme b as the product. Each …

Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen‐bonding interactions of the four propionate groups

T Gabler, F Sebastiani, J Helm, A Dali… - The FEBS …, 2022 - Wiley Online Library
Coproporpyhrin III is the substrate of coproporphyrin ferrochelatases (CpfCs). These
enzymes catalyse the insertion of ferrous iron into the porphyrin ring. This is the penultimate …

Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Heme b

L Milazzo, T Gabler, D Pühringer, Z Jandova… - ACS …, 2019 - ACS Publications
Coproheme decarboxylase (ChdC) catalyzes the last step in the heme biosynthesis pathway
of monoderm bacteria with coproheme acting both as redox cofactor and substrate …

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 …

Reaction intermediate rotation during the decarboxylation of coproheme to heme b in C. diphtheriae

F Sebastiani, H Michlits, B Lier, M Becucci… - Biophysical journal, 2021 - cell.com
Monoderm bacteria utilize coproheme decarboxylases (ChdCs) to generate heme b by a
stepwise decarboxylation of two propionate groups of iron coproporphyrin III (coproheme) …