Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 138, Issue 11, Pages 3631-3634Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.6b00017
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Funding
- NSF [CHE-1059084]
- NIH [1R01GM097200, GM 45617, GM 040541]
- Chemistry-Biology Interface Training Program [T32 GM 008496]
- University of California, Los Angeles
- Welch Foundation [F-1511]
- Direct For Mathematical & Physical Scien [1361104] Funding Source: National Science Foundation
- Division Of Chemistry [1361104] Funding Source: National Science Foundation
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SpnF, an enzyme involved in the biosynthesis of spinosyn A, catalyzes a transannular Diels-Alder reaction. Quantum mechanical computations and dynamic simulations now show that this cycloaddition is not well described as either a concerted or stepwise process, and dynamical effects influence the identity and timing of bond formation. The transition state for the reaction is ambimodal and leads directly to both the observed Diels-Alder and an unobserved [6+4] cycloadduct. The potential energy surface bifurcates and the cycloadditions occur by dynamically stepwise modes featuring an entropic intermediate. A rapid Cope rearrangement converts the [6+4] adduct into the observed [4+2] adduct. Control of nonstatistical dynamical effects may serve as another way by which enzymes control reactions.
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