Flavohaemoglobins were first described in yeast as early as the 1970s but their functions
were unclear. The surge in interest in nitric oxide biology and both serendipitous and …

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

Globin‐like oxygen‐binding proteins occur in bacteria, yeasts and other fungi, and protozoa.
The simplest contain protohaem as sole prosthetic group, but show considerable variation in …

Globins are an ancient and diverse superfamily of proteins. The globins of microorganisms
were relatively ignored for many decades after their discovery by Warburg in the 1930s and …

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 …

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

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

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 …

For more than a decade, the expression of Vitreoscilla hemoglobin (VHb) has been used to
improve the growth and/or productivity of various organisms that are important for the …

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