Cobalt is essential to the metabolism of all animals. It is a key constituent of cobalamin, also known as vitamin B, the primary biological reservoir of cobalt as an ultratrace element. Bacteria in the stomachs of ruminant animals convert cobalt salts into vitamin B, a compound which can only be produced by bacteria or archaea. A minimal presence of cobalt in soils therefore markedly improves the health of grazing animals, and an uptake of 0.20 mg/kg a day is recommended because they have no other source of vitamin B.
Proteins based on cobalamin use corrin to hold the cobalt. Coenzyme B features a reactive C-Co bond that participates in the reactions. In humans, B has two types of alkyl ligand: methyl and adenosyl. MeB promotes methyl (−CH) group transfers. The adenosyl version of B catalyzes rearrangements in which a hydrogen atom is directly transferred between two adjacent atoms with concomitant exchange of the second substituent, X, which may be a carbon atom with substituents, an oxygen atom of an alcohol, or an amine. Methylmalonyl coenzyme A mutase (MUT) converts MMl-CoA to Su-CoA, an important step in the extraction of energy from proteins and fats.
Although far less common than other metalloproteins (e.g. those of zinc and iron), other cobaltoproteins are known besides B. These proteins include methionine aminopeptidase 2, an enzyme that occurs in humans and other mammals that does not use the corrin ring of B, but binds cobalt directly. Another non-corrin cobalt enzyme is nitrile hydratase, an enzyme in bacteria that metabolizes nitriles.