In humans most cobalt is found in Vitamin B12. A cobalt atom is visible in the center in this diagram.
Cobalt is essential to the metabolism of all animals. It is a key constituent of cobalamin, also known as vitamin B12, the primary biological reservoir of cobalt as an ultratrace element.[1][2] Bacteria in the stomachs of ruminant animals convert cobalt salts into vitamin B12, 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 B12.[3]
Proteins based on cobalamin use corrin to hold the cobalt. Coenzyme B12 features a reactive C-Co bond that participates in the reactions.[4] In humans, B12 has two types of alkyl ligand: methyl and adenosyl. MeB12 promotes methyl (−CH3) group transfers. The adenosyl version of B12 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.[5]
Although far less common than other metalloproteins (e.g. those of zinc and iron), other cobaltoproteins are known besides B12. These proteins include methionine aminopeptidase 2, an enzyme that occurs in humans and other mammals that does not use the corrin ring of B12, but binds cobalt directly. Another non-corrin cobalt enzyme is nitrile hydratase, an enzyme in bacteria that metabolizes nitriles.[6]
^Yamada, Kazuhiro (2013). "Chapter 9. Cobalt: Its Role in Health and Disease". In Astrid Sigel; Helmut Sigel; Roland K. O. Sigel (eds.). Interrelations between Essential Metal Ions and Human Diseases. Metal Ions in Life Sciences. Vol. 13. Springer. pp. 295–320. doi:10.1007/978-94-007-7500-8_9. ISBN 978-94-007-7499-5. PMID 24470095.
^Cracan, Valentin; Banerjee, Ruma (2013). "Chapter 10 Cobalt and Corrinoid Transport and Biochemistry". In Banci, Lucia (ed.). Metallomics and the Cell. Metal Ions in Life Sciences. Vol. 12. Springer. pp. 333–374. doi:10.1007/978-94-007-5561-1_10. ISBN 978-94-007-5560-4. PMID 23595677. electronic-book ISBN 978-94-007-5561-1 ISSN 1559-0836 electronic-ISSN 1868-0402.
^Schwarz, F. J.; Kirchgessner, M.; Stangl, G. I. (2000). "Cobalt requirement of beef cattle – feed intake and growth at different levels of cobalt supply". Journal of Animal Physiology and Animal Nutrition. 83 (3): 121–131. doi:10.1046/j.1439-0396.2000.00258.x.
^Voet, Judith G.; Voet, Donald (1995). Biochemistry. New York: J. Wiley & Sons. p. 675. ISBN 0-471-58651-X. OCLC 31819701.
^Smith, David M.; Golding, Bernard T.; Radom, Leo (1999). "Understanding the Mechanism of B12-Dependent Methylmalonyl-CoA Mutase: Partial Proton Transfer in Action". Journal of the American Chemical Society. 121 (40): 9388–9399. doi:10.1021/ja991649a.
^Kobayashi, Michihiko; Shimizu, Sakayu (1999). "Cobalt proteins". European Journal of Biochemistry. 261 (1): 1–9. doi:10.1046/j.1432-1327.1999.00186.x. PMID 10103026.
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