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Biochemistry of B12-Cofactors in Human Metabolism

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Water Soluble Vitamins

Part of the book series: Subcellular Biochemistry ((SCBI,volume 56))

Abstract

Vitamin B12, the “antipernicious anaemia factor”, is a crystallisable cobalt-complex, which belongs to a group of unique “complete” corrinoids, named cobalamins (Cbl). In humans, instead of the “vitamin”, two organometallic B12-forms are coenzymes in two metabolically important enzymes: Methyl-cobalamin, the cofactor of methionine synthase, and coenzyme B12 (adenosyl-cobalamin), the cofactor of methylmalonyl-CoA mutase. The cytoplasmatic methionine synthase catalyzes the transfer of a methyl group from N-methyl-tetrahydrofolate to homocysteine to yield methionine and to liberate tetrahydrofolate. In the mitochondrial methylmalonyl-CoA mutase a radical process transforms methylmalonyl-CoA (a remains e.g. from uneven numbered fatty acids) into succinyl-CoA, for further metabolic use. In addition, in the human mitochondria an adenosyl-transferase incorporates the organometallic group of coenzyme B12. In all these enzymes, the bound B12-derivatives engage (or are formed) in exceptional organometallic enzymatic reactions. This chapter recapitulates the physiological chemistry of vitamin B12, relevant in the context of the metabolic transformation of B12-derivatives into the relevant coenzyme forms and their use in B12-dependent enzymes.

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Abbreviations

Ado:

5′-(deoxy)-adenosyl

AdoCbl:

5′-deoxy-5′-adenosyl-cobalamin (coenzyme B12, also named adenosyl-cobalamin)

Ado-ImCba:

5′-deoxy-5′-adenosyl-imidazolyl-cobamide

B12r:

cob(II)alamin

B12s:

cob(I)alamin

BDE:

(homolytic) bond dissociation energy

Cba:

cobamide

Cbl:

cobalamin (a DMB-cobamide)

CNCbl:

cyano-cobalamin (vitamin B12)

CN-ImCba:

cyano-imidazolyl-cobamide

DMB:

5,6-dimethylbenzimidazole

H2OCbl+ :

aquo-cobalamin (B12a)

HOCbl:

hydroxo-cobalamin

ImCba:

imidazolyl-cobamide

MeCbl:

methyl-cobalamin

Me-ImCba:

methyl-imidazolyl-cobamide

MetH:

methionine synthase (from E. coli)

MMCM:

methylmalonyl-CoA mutase (from Propionibacterium shermanii)

NHE:

normal hydrogen electrode

NMR:

nuclear magnetic resonance

SAM:

S-adenosyl-methionine (AdoMet)

UV/Vis:

ultraviolet/visible absorbance spectrum

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Acknowledgements

This work was supported by the Austrian National Science Foundation (project No P13595) and by the European Commission (project No HPRN-CT-2002-00195).

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  1. Institute of Organic Chemistry and Centre of Molecular Biosciences (CMBI), University of Innsbruck, Innsbruck, Austria

    Bernhard Kräutler

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  1. Imperial College of Science, Technology and Medicine, Royal Brompton & Harefield NHS Foundatio, Sydney Street, London, SW3 6NP, United Kingdom

    Olaf Stanger

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Kräutler, B. (2012). Biochemistry of B12-Cofactors in Human Metabolism. In: Stanger, O. (eds) Water Soluble Vitamins. Subcellular Biochemistry, vol 56. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-2199-9_17

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