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 …

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

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

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

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 …

Microbial flavohemoglobins (flavoHbs) and hemoglobins (Hbs) show large NO
dioxygenation rate constants ranging from 745 to 2900 μM− 1s− 1 suggesting a primal NO …

All hemoglobins catalyze a reaction in which heme-bound dioxygen reacts directly with
nitrogen monoxide (NO) to produce nitrate, resulting in the oxidation of the heme iron. This …

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

A variety of hemoglobins, including several microbial flavohemoglobins, enzymatically
dioxygenate the free radical nitric oxide (• NO) to form nitrate. Many of these• NO …

FeBMbs are structural and functional models of native bacterial nitric oxide reductases
(NORs) generated through engineering of myoglobin. These biosynthetic models replicate …