Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 111, Issue 10, Pages 2631-2638Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp066276w
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Funding
- Biotechnology and Biological Sciences Research Council [BB/D01963X/1, BB/C003896/1, BB/C511305/1, B19724/2] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BB/D01963X/1, B19724/2, BB/C003896/1, BB/C511305/1] Funding Source: Medline
- BBSRC [BB/D01963X/1] Funding Source: UKRI
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Hydrogen transfer, an essential component of most biological reactions, is a quantum problem. However, the proposed role of compressive motion in promoting enzymatic H-transfer is contentious. Using molecular dynamics simulations and density functional theory (DFT) calculations, we show that, during proton tunneling in the oxidative deamination of tryptamine catalyzed by the enzyme aromatic amine dehydrogenase (AADH), a sub-picosecond promoting vibration is inherent to the iminoquinone intermediate. We show by numerical modeling that this short-range vibration, with a frequency of similar to 165 cm(-1), is consistent with gating motion in the hydrogen tunneling model of Kuznetsov and Ulstrup (Kuznetsov, A. M.; Ulstrup, J. Can. J. Chem. 1999, 77, 1085) in an enzymatic reaction with an observed protium/deuterium kinetic isotope effect that is not measurably temperature-dependent.
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