Modified tetrapyrroles are large macrocyclic compounds, consisting of diverse conjugation
and metal chelation systems and imparting an array of colors to the biological structures that …

Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, poses a great threat
to human health. With the emergence of drug resistant Mtb strains, new therapeutics are …

Heme is an essential metabolite for most life on earth. Bacterial pathogens almost
universally require iron to infect a host, often acquiring this nutrient in the form of heme. The …

The Mycobacterium tuberculosis (Mtb) heme oxygenase MhuD liberates free iron by
degrading heme to the linear tetrapyrrole mycobilin. The MhuD dimer binds up to two hemes …

Staphylococcus aureus IsdG catalyzes a unique trioxygenation of heme to staphylobilin, and
the data presented in this article elucidate the mechanism of the novel chemical …

The noncanonical heme oxygenase MhuD from Mycobacterium tuberculosis binds a heme
substrate that adopts a dynamic equilibrium between planar and out-of-plane ruffled …

Rishirilides are a group of PKS II secondary metabolites produced by Streptomyces
bottropensis Gö C4/4. Biosynthetic studies in the past have elucidated early and late steps of …

The oxygen-dependent heme utilization degrading enzyme in Mycobacterium tuberculosis
(MhuD) uniquely integrates monooxygenase and dioxygenase functions in a single active …

Non-canonical heme oxygenases are enzymes that degrade heme to non-biliverdin
products within bacterial heme iron acquisition pathways. These enzymes all contain a …

Mycobacterium tuberculosis MhuD catalyzes the oxygenation of heme to mycobilin;
experimental data presented here elucidates the novel hydroxylation reaction catalyzed by …