Background: The first hemoglobin identified in bacteria was isolated from Vitreoscilla
stercoraria (VtHb) as a homodimeric species. The wild-type protein has been reported to …

Abstract The hemoglobin (VHb) from Vitreoscilla was the first bacterial hemoglobin
discovered. Its structure and function have been extensively investigated, and engineering …

In response to oxygen limitation or oxidative and nitrosative stress, bacteria express three
kinds of hemoglobin proteins: truncated hemoglobins (tr Hbs), hemoglobins (Hbs) and …

Truncated hemoglobins (trHbs) 1 (1) constitute a family of small oxygen-binding heme
proteins distributed in eubacteria, cyanobacteria, protozoa, and plants (Table I …

The hemoglobins found in unicellular organisms show a great deal of chemical reactivity,
protecting cells against oxidative stress, and hence have been implicated in a wider variety …

The hemoglobin from the bacterium Vitreoscilla (VHb) is the first microbial hemoglobin that
was conclusively identified as such (in 1986). It has been extensively studied with respect to …

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 …

A new truncated hemoglobin (HbO) from Mycobacterium tuberculosis has been expressed
and purified. Sequence alignment of HbO with other hemoglobins suggests that the proximal …

Two putative hemoglobin genes, glbN and glbO, were recently discovered in the complete
genome sequence of Mycobacterium tuberculosis H37Rv. Here, we show that the glbN …

Hemoglobins have been discovered in organisms from virtually all kingdoms. Their
presence in unicellular organisms suggests that the gene for hemoglobin is very ancient and …