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Lookup NU author(s): Emeritus Professor Bernard Golding
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The interconversion of (S)-glutamate and (2S,3S)-3-methylaspartate catalyzed by B-12-dependent glutamate mutase is discussed using results from high-level ab initio molecular orbital calculations. Evidence is presented regarding the possible role of coenzyme-B-12 in substrate activation and product formation via radical generation. Calculated electron paramagnetic resonance parameters support experimental evidence for the involvement of substrate-derived radicals and will hopefully aid the future detection of other important radical intermediates. The height of the rearrangement barrier for a fragmentation-recombination pathway, calculated with a model that includes neutral amino and carboxylic acid substituents in the migrating glycyl group, supports recent experimental evidence for the interconversion of (S)-glutamate and (2S,3S)-3-methylaspartate through such a pathway. Our calculations suggest that the enzyme may facilitate the rearrangement of (S)-glutamate through (partial) proton-transfer processes that control the protonation state of substituents in the migrating group.
Author(s): Wetmore SD, Smith DM, Golding BT, Radom L
Publication type: Article
Publication status: Published
Journal: Journal of the American Chemical Society
ISSN (print): 0002-7863
ISSN (electronic): 1520-5126
Publisher: American Chemical Society
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