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Title: Single Amino Acid Mutation Controls Hole Transfer Dynamics in DNA-Methyltransferase HhaI Complexes
Author: Corbella Morató, Marina
Voityuk, Alexander A.
Curutchet Barat, Carles E.
Keywords: Transferència d'energia
Transferència de càrrega
Reparació de l'ADN
Complexitat computacional
Energy transfer
Charge transfer
DNA repair
Computational complexity
Issue Date: 2-Sep-2015
Publisher: American Chemical Society
Abstract: Different mutagenic effects are generated by DNA oxidation that implies the formation of radical cation states (so-called holes) on purine nucleobases. The interaction of DNA with proteins may protect DNA from oxidative damage owing to hole transfer (HT) from the stack to aromatic amino acids. However, how protein binding affects HT dynamics in DNA is still poorly understood. Here, we report a computational study of HT in DNA complexes with methyltransferase HhaI with the aim of elucidating the molecular factors that explain why long-range DNA HT is inhibited when the glutamine residue inserted in the double helix is mutated into a tryptophan. We combine molecular dynamics, quantum chemistry, and kinetic Monte Carlo simulations and find that protein binding stabilizes the energies of the guanine radical cation states and significantly impacts the corresponding electronic couplings, thus determining the observed behavior, whereas the formation of a tryptophan radical leads to less efficient HT.
Note: Versió postprint del document publicat a:
It is part of: Journal of Physical Chemistry Letters, 2015, vol. 6, num. 18, p. 3749-3753
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ISSN: 1948-7185
Appears in Collections:Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica)

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