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 …

Chlorite is a serious environmental concern, as rising concentrations of this harmful
anthropogenic compound have been detected in groundwater, drinking water, and soil …

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

The chlorite dismutases (C-family proteins) are a widespread family of heme-binding
proteins for which chemical and biological roles remain unclear. An association of the gene …

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 …

Coproheme decarboxylases (ChdCs) are enzymes responsible for the catalysis of the
terminal step in the coproporphyrin-dependent heme biosynthesis pathway. Phylogenetic …

Heme b containing chlorite dismutase (Cld) catalyses the conversion of chlorite to chloride
and dioxygen which includes an unusual Osingle bondO bond formation. This review …

PFam Clan 0032, also known as the CDE superfamily, is a diverse group of at least 20
protein families sharing a common α, β-barrel domain. Of these, six different groups bind …

Chlorite dismutases (Clds) are heme b-containing oxidoreductases that convert chlorite to
chloride and dioxygen. In this work, the thermodynamics of the one-electron reduction of the …

Chlorite dismutases (Clds) are heme b containing oxidoreductases that convert chlorite to
chloride and molecular oxygen. In order to elucidate the role of conserved heme cavity …