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Lookup NU author(s): Antonius Pierik,
Professor Bernard Golding
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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.
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
ISSN (print): 1434-1948
ISSN (electronic): 1099-0682
Publisher: Wiley - VCH Verlag GmbH & Co. KGaA
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