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

Giardia lamblia is a pathogenic protist that infects the small intestine of mammals. As a
facultative anaerobe, Giardia obtains all of its energy by substrate-level phosphorylation …

Flavohemoglobins (flavoHbs) are enzymes that operate primarily as nitric oxide
dioxygenases and shuttle thereby electrons among NAD (P) H, FAD, heme, and a ligated …

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 …

Biochemical studies of flavohemoglobin (Hmp) from Escherichia coli suggest that instead of
aerobic oxygen delivery, a dioxygenase converts NO to NO 3− and anaerobically, an NO …

Flavohemoglobins (FHbs) are members of the globin superfamily, widely distributed among
prokaryotes and eukaryotes that have been shown to carry out nitric oxide dioxygenase …

Dimeric hemoglobin (VHb) from the bacterium Vitreoscilla sp. strain C1 displays 30 to 53%
sequence identity with the heme-binding domain of flavohemoglobins (flavoHbs) and …

Roseobacter denitrificans is a member of the widespread marine Roseobacter genus. We
report the first characterization of a truncated hemoglobin from R. denitrificans (Rd. trHb) that …

Flavohemoglobins (flavoHbs) are made of a globin domain fused with a ferredoxin
reductaselike FAD‐and NAD‐binding modules. These proteins are widely represented …

Flavohemoglobins (flavoHbs) serve various microorganisms as the major protective
enzymes against NO˙‐mediated toxicity. FlavoHbs dominantly function as an NO˙ …