Haem b and sirohaem are two iron-chelated modified tetrapyrroles that serve as prosthetic
groups in proteins with crucial roles in a variety of biological functions, such as gas transport …

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 …

Since the advent of protein crystallography, atomic-level macromolecular structures have
provided a basis to understand biological function. Enzymologists use detailed structural …

Myeloperoxidase (MPO) is synthesized by neutrophil and monocyte precursor cells and
contributes to host defense by mediating microbial killing. Although several steps in MPO …

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 …

Splitting the reduction potential of electron transport (ET) proteins and redox
metalloenzymes into the enthalpic and entropic contributions is an insightful practice to …

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 …

Coproheme decarboxylase (ChdC) catalyzes the last step in the heme biosynthesis pathway
of monoderm bacteria with coproheme acting both as redox cofactor and substrate …

Heme biosynthesis in Gram‐positive bacteria follows a recently described coproporphyrin‐
dependent pathway with HemQ catalyzing the decarboxylation of coproheme to heme b …

Coproporphyrin ferrochelatases (CpfCs, EC 4.99. 1.9) insert ferrous iron into coproporphyrin
III yielding coproheme. CpfCs are utilized by prokaryotic, mainly monoderm (Gram‐positive) …