The capacity of haem to transfer electrons, bind diatomic gases, and catalyse various
biochemical reactions makes it one of the essential biomolecules on Earth and one that was …

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 …

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 …

Genes for chlorite dismutase-like proteins are found widely among heme-synthesizing
bacteria and some Archaea. It is now known that among the Firmicutes and Actinobacteria …

Chlorite dismutase-like proteins are structurally closely related to functional chlorite
dismutases which are heme b-dependent oxidoreductases capable of reducing chlorite to …

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

Chlorite dismutases (Clds) are heme b-containing prokaryotic oxidoreductases that catalyze
the reduction of chlorite to chloride with the concomitant release of molecular oxygen. Over …

The heme enzyme chlorite dismutase (Cld) catalyzes the degradation of chlorite to chloride
and dioxygen. Although structure and steady-state kinetics of Clds have been elucidated …