| Abstract
| - Ab initio molecular orbital theory is used to investigate 1,2-amino shifts catalyzed by aminomutases,coenzyme B12, and vitamin B6 (in the form of pyridoxal 5‘-phosphate or PLP). Our calculations suggest essentialcatalytic roles for each of B12, B6, and the enzyme in aminomutase-catalyzed reactions. In the first place,coenzyme B12 provides a source of abstracting radicals, allowing the rearrangement reaction to take place onthe radical surface. The involvement of radicals is supported by comparison of experimental and theoreticalelectron paramagnetic resonance parameters. Next, B6 allows the enzyme to lower the barrier height byintroducing a double bond (allowing a low-energy intramolecular rearrangement pathway) and by providinga suitable site for partial protonation (preventing overstabilization of the reaction intermediate which couldlead to enzyme inactivation). The PLP hydroxyl group is also identified as an important participant in thesereactions. Finally, the enzyme holds the various reaction components in place and is the source of acidicfunctional groups that can provide partial protonation.
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