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Lookup NU author(s): Daniele Ciceri,
Professor Bernard Golding
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2-Methylideneglutarate mutase is an adenosylcobalamin (coenzyme B12)-dependent enzyme that catalyses the equilibration of 2-methylideneglutarate with (R)-3-methylitaconate. This reaction is believed to occur via protein-bound free radicals derived from substrate and product. The stereochemistry of the formation of the methyl group of 3-methylitaconate has been probed using a 'chiral methyl group'. The methyl group in 3-([2H1,3H]methyl)itaconate derived from either (R)- or (S)-2-methylidene[3-2H1,3-3H1]glutarate was a 50 : 50 mixture of (R)- and (S)-forms. It is concluded that the barrier to rotation about the C-C bond between the methylene radical centre and adjacent C-atom in the product-related radical [CH2CH(-O2CC=CH2)CO2-] is relatively low, and that the interaction of the radical with cob(1I)alamin is minimal. Hence, cob(I1)alamin is a spectator of the molecular rearrangement of the substrate radical to product radical.
Author(s): Ciceri D, Pierik AJ, Hartrampf G, Broker G, Speranza G, Buckel W, Cornforth SJ, Golding BT
Publication type: Article
Publication status: Published
Journal: Helvetica Chimica Acta
ISSN (print): 0018-019X
ISSN (electronic): 1522-2675
Publisher: Verlag Helvetica Chimica Acta
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