In this work we review the application of classical and quantum-mechanical atomistic
computer simulation tools to the investigation of small ligand interaction with globins. In the …

Bacterial pathogens have sophisticated systems that allow them to survive in hosts in which
innate immunity is the frontline of defense. One of the substances produced by infected …

Among 20 p450s of Mycobacterium tuberculosis (Mt), CYP121 has received an outstanding
interest, not only due to its essentiality for bacterial viability but also because it catalyzes an …

The Trypanosoma cruzi ascorbate peroxidase is, by sequence analysis, a hybrid type A
member of class I heme peroxidases [Tc APx-cytochrome c peroxidase (CcP)], suggesting …

Nitric-oxide dioxygenases (NODs) activate and combine O2 with NO to form nitrate. A variety
of oxygen-binding hemoglobins with associated partner reductases or electron donors …

Many pathogenic microorganisms have evolved hemoglobin-mediated nitric oxide (NO)
detoxification mechanisms, where a globin domain in conjunction with a partner reductase …

The substrates O 2 and NO cooperatively activate the NO dioxygenase function of
Escherichia coli flavohemoglobin. Steady-state and transient kinetic measurements support …

Two flavohemoglobins, type I and type II, displaying distinct structural features and cofactor
binding sites coexist in Mycobacterium smegmatis; however, none of these …

Flavohemoglobins are microbial enzymes that counter nitrosative stress, but the details of
their underlying enzymatic activities and structure–function relationships are not completely …

Flavohemoglobins (fHbs) are heme proteins found in prokaryotic and eukaryotic microbes.
They are involved in NO detoxification through an NO˙ dioxygenase mechanism. The N …