[1] P. furiosus belongs to the Pyrococcus genus, most commonly found in extreme environmental conditions of hydrothermal vents.

Certain superoxide dismutases found in P. furiosus can be introduced into plants to increase their tolerance in environmentally stressful conditions and ultimately their survival.

[3] Pyrococcus furiosus is a strictly anaerobic, heterotrophic, sulfur-reducing archaea originally isolated from heated sediments in Vulcano, Italy by Fiala and Stetter.

They are additionally utilized as cable-like connectors to adhere to various solid surfaces such as sand grains in the habitat in which this species was discovered.

The presence of hydrogen severely inhibits its growth and metabolism; this effect can be circumvented, however, by introducing sulfur into the organism's environment.

The Maryland team found that the genome has 1,908 kilobases, including 2,065 open reading frames (ORFs) that encode proteins.

[8] Pyrococcus furiosus possesses several highly thermostable alcohol dehydrogenases (ADHs): the short-chain AdhA, the iron-containing AdhB, the zinc-containing AdhC, and more.

[17] There is also the indolepyruvate ferredoxin oxidoreductase, or IOR, which utilizes iron and sulfur to catalyze the "oxidative decarboxylation of aryl pyruvates.

[22] However, since purified Taq DNA polymerase lacks exonuclease (proofreading) activity, it cannot excise mismatched nucleotides.

Researchers discovered in the early 1990s that the Pfu DNA polymerase of P. furiosus does actually possess a requisite 3’-to-5’ exonuclease activity allowing for the removal of errors.

It may be possible to use the enzymes of P. furiosus for applications in such industries as food, pharmaceuticals, and fine-chemicals in which alcohol dehydrogenases are necessary in the production of enantio- and diastereomerically pure diols.

Consequently, in this case, the specific enzyme AdhA was taken from P. furiosus and put through various mutations in a laboratory in order to obtain a suitable alcohol dehydrogenase for use in artificial processes.

This allowed scientists to obtain a mutant enzyme that could function efficiently at lower temperatures and maintain productivity.

In response to environmental stresses such as heat exposure, plants produce reactive oxygen species which can result in cell death.

Using two hyperthermophilic species of archaea lessens the possibility of deviations having to do with temperature of the environment, essentially reducing the variables in the experimental design.

[25] Besides yielding information about the barophilicity of certain amino acids, the experiment also provided valuable insight into the origin of the genetic code and its organizational influences.

[25] Pyrococcus furiosus was originally isolated anaerobically from geothermal marine sediments with temperatures between 90 °C (194 °F) and 100 °C (212 °F) collected at the beach of Porto Levante, Vulcano Island, Italy.

[1] The name Pyrococcus means "fireball" in Greek, to refer to the extremophile's round shape and ability to grow in temperatures of around 100 degrees Celsius.