Heme biosynthesis in the Gram-positive bacteria occurs mostly via a pathway that is distinct
from that of eukaryotes and Gram-negative bacteria in the three terminal heme synthesis …

Aggregated bacteria embedded within self-secreted extracellular polymeric substances, or
biofilms, are resistant to antibiotics and cause chronic infections. As such, they are a …

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 …

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 …

Mycobacterium tuberculosis heme-degrading protein MhuD degrades heme to mycobilin
isomers and iron, while its closest homologues from Staphylococcus aureus, IsdG and IsdI …

MhuD is a noncanonical heme oxygenase (HO) from Mycobacterium tuberculosis (Mtb) that
catalyzes unique heme degradation chemistry distinct from canonical HOs, generating …

HupZ is an expected heme degrading enzyme in the heme acquisition and utilization
pathway in Group A Streptococcus. The isolated HupZ protein containing a C-terminal V5 …

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

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

Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, requires iron for
survival. In Mtb, MhuD is the cytosolic protein that degrades imported heme. MhuD is …