Structural Biochemistry/Protein function/Heme group/Globins

It is an ancient and diverse family of protein. The globins of microorganisms were ignored and discovered in 1930s and rediscovered in 1950. Modern focus on them has been inspired by their structural diversity and fine-tuning to fulfill discrete functions. at least three classes of microbial globin are recognized, all have the classic globins’ protein fold.

First is the myoglobin like haemprotein Vgb from the bacterium vitreoscilla, which is unique because of its ability to improve growth and metabolism for biotechnological gain in a variety of host cells, even though its physiological function is not well understood yet. It has roles in oxygen but the metabolism has not been proposed yet for the 2nd type of globin- truncated globins, that is disguished because it is 20-40 residues shorter than Vgb. the third and the most well understood one is called flavohaemoglobins, it was partly characterized in yeast. they are characterized by the presence of an additional domain with binding sites for FAD and NAD(P)H. they are widely spread in bacteria.

A full understanding of microbial globins promises advances in controlling the interactions of pathogenic bacteria with their animal and plant hosts, and manipulation of microbial oxygen transfer with biotechnological applications.