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

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 …

Escherichia coli expresses an inducible flavohemoglobin possessing robust NO
dioxygenase activity. At 37° C, the enzyme shows a maximal turnover number (V max) of …

Kinetic and structural investigations of the flavohemoglobin-type NO dioxygenase have
suggested critical roles for transient Fe (III) O 2 complex formation and O 2-forced …

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

Members of the hemoglobin superfamily efficiently catalyze nitric-oxide dioxygenation, and
when paired with native electron donors, function as NO dioxygenases (NODs). Indeed, the …

Distantly related members of the hemoglobin (Hb) superfamily including red blood cell Hb,
muscle myoglobin (Mb) and the microbial flavohemoglobin (flavoHb) dioxygenate nitric …

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

Widely distributed flavohemoglobins (flavoHbs) function as NO dioxygenases and confer
upon cells a resistance to NO toxicity. FlavoHbs from Saccharomyces cerevisiae …

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