A purification procedure for flavohaemoglobin Hmp (NO oxygenase) is described that gives
high yields of protein with equistoichiometric haem and FAD contents. H2O2 accumulated …

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

Flavohemoglobins, which are widely distributed in prokaryotes and eukaryotes, play key
roles in oxygen (O2) transport and nitric oxide (· NO) defense. Hmp is the flavohemoglobin of …

Two distantly related flavohemoglobins (FHbs), MsFHbI and MsFHbII, having crucial
differences in their heme and reductase domains, co-exist in Mycobacterium smegmatis …

Over the past decade, the flavohemoglobin Hmp has emerged as the most significant nitric
oxide (NO)–detoxifying protein in many diverse organisms, including yeasts and fungi but …

Being an obligate aerobe, Mycobacterium tuberculosis faces a number of energetic
challenges when it encounters hypoxia and environmental stress during intracellular …

The Escherichia coli haemoglobin-like flavohaemoprotein (Hmp) has been purified to near
homogeneity using two chromatographic steps. The prosthetic groups are identified as FAD …

Flavohemoglobin was isolated directly from the yeast Candida norvegensis and studied on
its structural, spectral, and stability properties. In Candidaflavohemoglobin, the 155 N …

The molecular structure of the flavohemoglobin from Alcaligenes eutrophus has been
determined to a resolution of 1.75 A and refined to an R‐factor of 19.6%. The protein …

Kinetic studies were performed on ligand rebinding to a cold-adapted globin of the Antarctic
bacterium Pseudoalteromonas haloplanktis TAC125 (Ph-2/2HbO). This 2/2 hemoglobin …