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• W2048657980 abstract "We have applied local density functional theory, an ab initio quantum mechanical method, to study the shift in the spatial electron density of the substrate dihydrofolate that accompanies binding to the enzyme dihydrofolate reductase. The results shed light on fundamental electronic effects due to the enzyme that may contribute to catalysis. In particular, the enzyme induces a long-range polarization of the substrate that perturbs its electron density distribution in a specific and selective way in the vicinity of the bond that is reduced by the enzyme. Examination of the electron density changes that occur in folate reveals that a similar effect is seen but this time specifically at the bond that is reduced in this substrate. This suggests that the polarization effect may be implicated in the reaction mechanism and may play a role in determining the sequence whereby the 7,8-bond in folate is reduced first, followed by reduction of the 5,6-bond in the resulting dihydro compound." @default.
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• W2048657980 date "1991-08-01" @default.
• W2048657980 modified "2023-09-26" @default.
• W2048657980 title "Theoretical studies on the dihydrofolate reductase mechanism: electronic polarization of bound substrates." @default.
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• W2048657980 doi "https://doi.org/10.1073/pnas.88.15.6423" @default.
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