[2] First discovered in the sediment of a marine geothermal area near Vulcano, Italy, Thermotoga maritima resides in hot springs as well as hydrothermal vents.

[4] Thermotoga maritima is the only bacterium known to grow at this high a temperature; the only other organisms known to live in environments this extreme are members of the domain Archaea.

[6] T. maritima is also capable of metabolizing cellulose as well as xylan, yielding H2 that could potentially be utilized as an alternative energy source to fossil fuels.

[7] Collectively, these attributes indicate that T. maritima has become resourceful and capable of metabolizing a host of substances in order to carry out its life processes.

However, similar to other fermentative bacteria, the biohydrogen yield in this bacterium does not go beyond 4 mol H2 / glucose (Thaeur limit) because of its inherent nature to use more energy for its own cell division to grow rapidly than producing H2.

Overcoming this limit by improving the conversion of sugar to H2 could lead to a superior H2 producing biological system that may supersede fossil fuel-based H2 production.

Metabolic engineering in this bacterium led to development of strains of T. maritima that surpassed the Thauer limit of hydrogen production.

In this strain, energy redistribution, and metabolic rerouting through the pentose phosphate pathway (PPP) generated excess reductants while uncoupling growth from hydrogen synthesis.

[9] Within its genome it has several heat and cold shock proteins that are most likely involved in metabolic regulation and response to environmental temperature changes.

[13] Developing a genetic system for T. maritima has been a challenging task primarily because of a lack of a suitable heat-stable selectable marker.

[14] This newly developed genetic system relies upon a pyrE− mutant that was isolated after cultivating T. maritima on a pyrimidine biosynthesis inhibiting drug called 5-fluoroorotic acid (5-FOA).

Recently developed genetic system in T. maritima has been very useful to determine the function of the ATPase protein (MalK) of the maltose transporter that is present in a multi-copy (three copies) fashion.