@inproceedings{3f1205a94f14406081433566fc202454,
title = "Role of fluctuations in quinone reductase hydride transfer: A combined quantum mechanics and molecular dynamics study",
abstract = "Quinone Reductase is a cytosolic FAD-containing enzyme that carries out the obligatory two-electron reduction of quinones to hydroquinones. The first step in the mechanism consists of the reduction of the FAD by NAD(P)H via direct a hydride transfer. Combined QM/MM calculations show that the protein accelerates this step by a combination of effects that include charge stabilization and distortion. The calculations also show that dynamic effects play an important role in QR catalysis: the distance between the donor and the acceptor atoms of the hydride transfer, which is too long for transfer in the static structure, becomes shorter than 3 {\AA} 25% of the time due to motions of the protein and the cofactors.",
keywords = "DT-diaphorase, Density functional, Enzymes, Flavoproteins, Isoalloxazine, Molecular dynamics, Protein fluctuations, Quantum chemistry",
author = "German Cavelier and Amzel, {L. Mario}",
year = "2006",
doi = "10.1063/1.2345619",
language = "English (US)",
isbn = "0735403503",
series = "AIP Conference Proceedings",
pages = "1--15",
booktitle = "FROM PHYSICS TO BIOLOGY",
note = "FROM PHYSICS TO BIOLOGY: The Interface between Experiment and Computation - BIFI 2006 II International Congress ; Conference date: 08-02-2006 Through 11-02-2006",
}