Toggle Main Menu Toggle Search

Open Access padlockePrints

Mechanism-based inactivation of coenzyme B12-dependent 2-methyleneglutarate mutase by (Z)-glutaconate and buta-1,3-diene-2,3- dicarboxylate

Lookup NU author(s): Antonius Pierik, Diana Suarez, Shang-Min Tu, Emeritus Professor Bernard Golding


Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


In the presence of holo 2-methyleneglutarate mutase, buta-1,3-diene-2,3- dicarboxylate and (Z)-glutaconate [(Z)-pent-2-ene-1,5-dicarboxylate], but not (E)-glutaconate, each induced homolysis of the Co-C bond of coenzyme B 12 to afford cob(II)alamin and the 5′-deoxyadenosyl radical. The latter probably added to the double bond in (Z)-glutaconate and one of the double bonds in buta-1,3-diene-2,3-dicarboxylate to afford a corresponding "radical adduct". The formation of new radicals and cob(II)alamin was diagnosed by UV/Visible and EPR spectroscopy. (Z)-Glutaconate rapidly inactivated the mutase with formation of aquocobalamin, which was possibly derived by electron transfer from cob(II)alamin to the radical adduct. In contrast, buta-1,3-diene-2,3-dicarboxylate was a much slower inactivator. In this case, the spectroscopic data revealed a relatively stable complex of the radical adduct with cob(II)alamin in the active site of the enzyme. © Wiley-VCH Verlag GmbH & Co. KGaA, 2006.

Publication metadata

Author(s): Buckel W, Pierik AJ, Plett S, Alhapel A, Suarez D, Tu S-M, Golding BT

Publication type: Article

Publication status: Published

Journal: European Journal of Inorganic Chemistry

Year: 2006

Issue: 18

Pages: 3622-3626

ISSN (print): 1434-1948

ISSN (electronic): 1099-0682

Publisher: Wiley - VCH Verlag GmbH & Co. KGaA


DOI: 10.1002/ejic.200600405


Altmetrics provided by Altmetric