The biochemical diversity of life near and above 100°C in marine environments

• Published in: Journal of applied microbiology Vol. 85; no. S1; pp. 108S - 117S
• Main Author: Adams, M.W.W.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01-12-1998
• Subjects: Archaea - enzymology; Archaea - metabolism; Bacteria, Anaerobic - enzymology; Bacteria, Anaerobic - metabolism; Biodiversity; Fermentation; Hot Temperature; Oceans and Seas; Oxidation-Reduction; Oxidoreductases - metabolism; Seawater - microbiology; Tungsten - metabolism; Water Microbiology
• ISSN: 1364-5072; 1365-2672
• DOI: 10.1111/j.1365-2672.1998.tb05289.x

SUMMARY
Hyperthermophilic micro‐organisms grow at temperatures above 90 °C with a current upper limit of 113 °C. They are a recent discovery in the microbial world and have been isolated mainly from marine geothermal environments, which include both shallow and deep sea hydrothermal vents. By 16S rRNA analyses they are the most slowly evolving of all extant life forms, and all but two of the nearly 20 known genera are classified as Archaea (formerly Archaebacteria). Almost all hyperthermophiles are strict anaerobes. They include species of methanogens, iron‐oxidizers and sulphate reducers, but the majority are obligate heterotrophs that depend upon the reduction of elemental sulphur (S°) to hydrogen sulphide for significant growth. The heterotrophs utilize proteinaceous materials as carbon and energy sources, although a few species are also saccharolytic. A scheme for electron flow during the oxidation of carbohydrates and peptides and the reduction of S° has been proposed. Two S°‐reducing enzymes have been purified from the cytoplasm of one hyperthermophile (Topt 100 °C) that is able to grow either with and without S°. However, the mechanisms by which S° reduction is coupled to energy conservation in this organism and in obligate S°‐reducing hyperthermophiles is not known. In the heterotrophs, sugar fermentation is achieved by a novel glycolytic pathway involving unusual ADP‐dependent kinases and ATP synthetases, and novel oxidoreductases that are ferredoxin‐ rather than NAD(P)‐linked. Similarly, peptide fermentation involves several unusual ferredoxin‐linked oxidoreductases not found in mesophilic organisms. Several of these oxido‐reductases contain tungsten, an element that is rarely used in biological systems. Tungsten is present in exceedingly low concentrations in normal sea water, but hydrothermal systems contain much higher tungsten concentrations, more than sufficient to support hyperthermophilic life.