Tungsten is one of the oldest metal ions to be incorporated in biological systems, preceding the Great Oxygenation Event. Before the abundance of oxygen in Earth's atmosphere, oceans teemed with sulfur and tungsten, while molybdenum, a metal that is highly similar chemically, was inaccessible in solid form. The abundance of tungsten and lack of free molybdenum likely explains why early marine organisms incorporated the former instead of the latter. However, as cyanobacteria began to fill the atmosphere with oxygen, molybdenum became available (molybdenum becomes soluble when exposed to oxygen) and molybdenum began to replace tungsten in the majority of metabolic processes, which is seen today, as tungsten is only present in the biological complexes of prokaryotes (methanogens, gram-positive bacteria, gram-negative aerobes and anaerobes), and is only obligated in hyperthermophilic archaea such as P. furiosus.
Although research into the specific enzyme complexes in which tungsten is incorporated is relatively recent (1970s), natural tungstoenzymes are abundantly found in a large number of prokaryotic microorganisms. These include formate dehydrogenase, formyl methanufuran dehydrogenase, acetylene hydratase, and a class of phylogenetically related oxidoreductases that catalyze the reversible oxidation of aldehydes. The first crystal structure of a tungsten- or pterin-containing enzyme, that of aldehyde ferredoxin oxidoreductase from P. furiosus, has revealed a catalytic site with one W atom coordinated to two pterin molecules which are themselves bridged by a magnesium ion.