Bacterial hemoglobins and flavohemoglobins: versatile proteins and their impact on microbiology and biotechnology.
In response to oxygen limitation or oxidative and nitrosative stress, bacteria express three kinds of hemoglobin proteins: truncated hemoglobins (tr Hbs), hemoglobins (Hbs) and flavohemoglobins (flavo Hbs). The two latter groups share a high sequence homology and structural similarity in their globin domain. Flavohemoglobin proteins contain an additional reductase domain at their C-terminus and their expression is induced in the presence of reactive nitrogen and oxygen species. Flavohemoglobins detoxify NO in an aerobic process, termed nitric oxide dioxygenase reaction, which protects the host from various noxious nitrogen compounds. Only a small number of bacteria express hemoglobin proteins and the best studied of these is from Vitreoscilla sp. Vitreoscilla hemoglobin (VHb) has been expressed in various heterologous hosts under oxygen-limited conditions and has been shown to improve growth and productivity, rendering the protein interesting for biotechnology industry. The close interaction of VHb with the terminal oxidases has been shown and this interplay has been proposed to enhance respiratory activity and energy production by delivering oxygen, the ultimate result being an improvement in growth properties.
Frey
Alexander D
AD
Institute of Biotechnology, ETH Zürich, 8093 Zürich, Switzerland.
Kallio
Pauli T
PT
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism*; D001709:Biotechnology; D006420:Hemeproteins / Q000235:genetics* / Q000378:metabolism*; D006454:Hemoglobins / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D009569:Nitric Oxide / Q000378:metabolism; D054793:Truncated Hemoglobins
D001426:Bacterial Proteins; D006420:Hemeproteins; D006454:Hemoglobins; D054793:Truncated Hemoglobins; C086193:flavohemoprotein, Bacteria; D009569:Nitric Oxide