Cobalt in biology

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In humans most cobalt is found in Vitamin B12. A cobalt atom is visible in the center in this diagram. Cobalamin skeletal.svg
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]

Cobalt deficiency

In humans, consumption of cobalt-containing vitamin B12 meets all needs for cobalt. For cattle and sheep, which meet vitamin B12 needs via synthesis by resident bacteria in the rumen, there is a function for inorganic cobalt. In the early 20th century, during the development of farming on the North Island Volcanic Plateau of New Zealand, cattle suffered from what was termed "bush sickness". It was discovered that the volcanic soils lacked the cobalt salts essential for the cattle food chain. [7] [8] The "coast disease" of sheep in the Ninety Mile Desert of the Southeast of South Australia in the 1930s was found to originate in nutritional deficiencies of trace elements cobalt and copper. The cobalt deficiency was overcome by the development of "cobalt bullets", dense pellets of cobalt oxide mixed with clay given orally for lodging in the animal's rumen.[ clarification needed ] [9] [8] [10]

Related Research Articles

Metalloprotein Protein that contains a metal ion cofactor

Metalloprotein is a generic term for a protein that contains a metal ion cofactor. A large proportion of all proteins are part of this category. For instance, at least 1000 human proteins contain zinc-binding protein domains although there may be up to 3000 human zinc metalloproteins.

Methylmalonic acidemia Medical condition

Methylmalonic acidemia, also called methylmalonic aciduria, is an autosomal recessive metabolic disorder that disrupts normal amino acid metabolism. It is a classical type of organic acidemia. The result of this condition is the inability to properly digest specific fats and proteins, which in turn leads to a buildup of a toxic level of methylmalonic acid in the blood.

Bioinorganic chemistry is a field that examines the role of metals in biology. Bioinorganic chemistry includes the study of both natural phenomena such as the behavior of metalloproteins as well as artificially introduced metals, including those that are non-essential, in medicine and toxicology. Many biological processes such as respiration depend upon molecules that fall within the realm of inorganic chemistry. The discipline also includes the study of inorganic models or mimics that imitate the behaviour of metalloproteins.

Methylmalonyl-CoA mutase deficiency Medical condition

Methylmalonyl-CoA mutase is a mitochondrial homodimer apoenzyme that focuses on the catalysis of methylmalonyl CoA to succinyl CoA. The enzyme is bound to adenosylcobalamin, a hormonal derivative of vitamin B12 in order to function. Methylmalonyl-CoA mutase deficiency is caused by genetic defect in the MUT gene responsible for encoding the enzyme. Deficiency in this enzyme accounts for 60% of the cases of methylmalonic acidemia.

Methylcobalamin

Methylcobalamin (mecobalamin, MeCbl, or MeB12) is a cobalamin, a form of vitamin B12. It differs from cyanocobalamin in that the cyano group at the cobalt is replaced with a methyl group. Methylcobalamin features an octahedral cobalt(III) centre and can be obtained as bright red crystals. From the perspective of coordination chemistry, methylcobalamin is notable as a rare example of a compound that contains metal–alkyl bonds. Nickel–methyl intermediates have been proposed for the final step of methanogenesis.

Corrinoid Class of chemical compounds

Corrinoids are a group of compounds based on the skeleton of corrin, a cyclic system containing four pyrrole rings similar to porphyrins. These include compounds based on octadehydrocorrin, which has the trivial name corrole.

Methylmalonyl-CoA mutase

Methylmalonyl-CoA mutase (MCM), mitochondrial, also known as methylmalonyl-CoA isomerase, is a protein that in humans is encoded by the MUT gene. This vitamin B12-dependent enzyme catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA in humans. Mutations in MUT gene may lead to various types of methylmalonic aciduria.

Hydroxocobalamin

Hydroxocobalamin, also known as vitamin B12a and hydroxycobalamin, is a vitamin found in food and used as a dietary supplement. As a supplement it is used to treat vitamin B12 deficiency including pernicious anemia. Other uses include treatment for cyanide poisoning, Leber's optic atrophy, and toxic amblyopia. It is given by injection into a muscle or vein.

Methylmalonyl-CoA Chemical compound

Methylmalonyl-CoA is the thioester consisting of coenzyme A linked to methylmalonic acid. It is an important intermediate in the biosynthesis of succinyl-CoA, which plays an essential role in the tricarboxylic acid cycle. The compound is sometimes referred to as "methylmalyl-CoA".

In enzymology, nitrile hydratases are mononuclear iron or non-corrinoid cobalt enzymes that catalyse the hydration of diverse nitriles to their corresponding amides

Adenosylcobalamin

Adenosylcobalamin (AdoCbl), also known as coenzyme B12, cobamamide, and dibencozide, is, along with methylcobalamin (MeCbl), one of the biologically active forms of vitamin B12.

In enzymology, a cobalt-factor II C20-methyltransferase is an enzyme that catalyzes the chemical reaction

Precorrin-2 C20-methyltransferase

In enzymology, a precorrin-2 C20-methyltransferase is an enzyme that catalyzes the chemical reaction

Precorrin-3B C17-methyltransferase

In enzymology, precorrin-3B C17-methyltransferase is an enzyme that catalyzes the chemical reaction

Vitamin B<sub><small>12</small></sub> Vitamin used in animal cells metabolism

Vitamin B12, also known as cobalamin, is a water-soluble vitamin involved in metabolism. It is one of eight B vitamins. It is required by animals, which use it as a cofactor in DNA synthesis, in both fatty acid and amino acid metabolism. It is important in the normal functioning of the nervous system via its role in the synthesis of myelin, and in the circulatory system in the maturation of red blood cells in the bone marrow. Plants do not need cobalamin and carry out the reactions with enzymes that are not dependent on it.

Cyanocobalamin Manufactured form of vitamin B-12

Cyanocobalamin is a manufactured form of vitamin B
12 used to treat vitamin B
12 deficiency. The deficiency may occur in pernicious anemia, following surgical removal of the stomach, with fish tapeworm, or due to bowel cancer. It is less preferred than hydroxocobalamin for treating vitamin B
12 deficiency. It is used by mouth, by injection into a muscle, or as a nasal spray.

Cobalt Chemical element, symbol Co and atomic number 27

Cobalt is a chemical element with the symbol Co and atomic number 27. As with nickel, cobalt is found in the Earth's crust only in a chemically combined form, save for small deposits found in alloys of natural meteoric iron. The free element, produced by reductive smelting, is a hard, lustrous, silver-gray metal.

Vitamin B12-binding domain Type of protein domain

In molecular biology, the vitamin B12-binding domain is a protein domain which binds to cobalamin. It can bind two different forms of the cobalamin cofactor, with cobalt bonded either to a methyl group (methylcobalamin) or to 5'-deoxyadenosine (adenosylcobalamin). Cobalamin-binding domains are mainly found in two families of enzymes present in animals and prokaryotes, which perform distinct kinds of reactions at the cobalt-carbon bond. Enzymes that require methylcobalamin carry out methyl transfer reactions. Enzymes that require adenosylcobalamin catalyse reactions in which the first step is the cleavage of adenosylcobalamin to form cob(II)alamin and the 5'-deoxyadenosyl radical, and thus act as radical generators. In both types of enzymes the B12-binding domain uses a histidine to bind the cobalt atom of cobalamin cofactors. This histidine is embedded in a DXHXXG sequence, the most conserved primary sequence motif of the domain. Proteins containing the cobalamin-binding domain include:

Cobalamin biosynthesis

Cobalamin biosynthesis is the process by which bacteria and archea make cobalamin, vitamin B12. Many steps are involved in converting aminolevulinic acid via uroporphyrinogen III and adenosylcobyric acid to the final forms in which it is used by enzymes in both the producing organisms and other species, including humans who acquire it through their diet.

Cobalt-precorrin-5B (C1)-methyltransferase (EC 2.1.1.195), cobalt-precorrin-6A synthase, CbiD (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:cobalt-precorrin-5B (C1)-methyltransferase. This enzyme catalyses the following chemical reaction

References

  1. ↑ 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. PMID   24470095.
  2. ↑ 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.
  3. ↑ 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.
  4. ↑ Voet, Judith G.; Voet, Donald (1995). Biochemistry . New York: J. Wiley & Sons. p.  675. ISBN   0-471-58651-X. OCLC   31819701.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ "Soils". Waikato University. Archived from the original on 2012-01-25. Retrieved 2012-01-16.
  8. 1 2 McDowell, Lee Russell (2008). Vitamins in Animal and Human Nutrition (2nd ed.). Hoboken: John Wiley & Sons. p. 525. ISBN   978-0-470-37668-3.
  9. ↑ Australian Academy of Science > Deceased Fellows > Hedley Ralph Marston 1900–1965 Accessed 12 May 2013.
  10. ↑ Snook, Laurence C. (1962). "Cobalt: its use to control wasting disease". Journal of the Department of Agriculture, Western Australia. 4. 3 (11): 844–852.
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