Nitric oxide (NO•) is a toxin, and various life forms appear to have evolved strategies for its
detoxification. NO•-resistant mutants of Escherichia coli were isolated that rapidly consumed …

Nitric-oxide dioxygenase (NOD) and reductase (NOR) activities of flavohemoglobin
(flavoHb) have been suggested as mechanisms for NO metabolism and detoxification in a …

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

We have previously reported that bacterial flavohemoglobin (HMP) catalyzes both a rapid
reaction of heme-bound O2 with nitric oxide (NO) to form nitrate [HMP-Fe (II) O2+ NO→ HMP …

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

Hemoglobin homologs are being identified in an expanding number of unicellular
prokaryotic and eukaryotic organisms. Many of these hemoglobins are twodomain proteins …

Flavohemoglobins metabolize nitric oxide (NO) to nitrate and protect bacteria and fungi from
NO-mediated damage, growth inhibition, and killing by NO-releasing immune cells …

Respiration of Escherichia colicatalyzed either by cytochrome bo′ or bd is sensitive to
micromolar extracellular NO; extensive, transient inhibition of respiration increases as …

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

Yeast hemoglobin was discovered close to half a century ago, but its function has remained
unknown. Herein, we report that this flavohemoglobin protects Saccharomyces cerevisiae …