% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Genna:820729,
      author       = {Genna, Vito and Vidossich, Pietro and Ippoliti, Emiliano
                      and Carloni, Paolo and Vivo, Marco De},
      title        = {{A} {S}elf-{A}ctivated {M}echanism for {N}ucleic {A}cid
                      {P}olymerization {C}atalyzed by {DNA}/{RNA} {P}olymerases},
      journal      = {Journal of the American Chemical Society},
      volume       = {138},
      number       = {44},
      issn         = {1520-5126},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2016-05997},
      pages        = {14592 - 14598},
      year         = {2016},
      abstract     = {The enzymatic polymerization of DNA and RNA is the basis
                      for genetic inheritance for all living organisms. It is
                      catalyzed by the DNA/RNA polymerase (Pol) superfamily. Here,
                      bioinformatics analysis reveals that the incoming nucleotide
                      substrate always forms an H-bond between its 3′-OH and
                      β-phosphate moieties upon formation of the Michaelis
                      complex. This previously unrecognized H-bond implies a novel
                      self-activated mechanism (SAM), which synergistically
                      connects the in situ nucleophile formation with subsequent
                      nucleotide addition and, importantly, nucleic acid
                      translocation. Thus, SAM allows an elegant and efficient
                      closed-loop sequence of chemical and physical steps for Pol
                      catalysis. This is markedly different from previous
                      mechanistic hypotheses. Our proposed mechanism is
                      corroborated via ab initio QM/MM simulations on a specific
                      Pol, the human DNA polymerase-η, an enzyme involved in
                      repairing damaged DNA. The structural conservation of DNA
                      and RNA Pols supports the possible extension of SAM to Pol
                      enzymes from the three domains of life.},
      cin          = {IAS-5 / INM-9},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000387625300018},
      pubmed       = {pmid:27530537},
      doi          = {10.1021/jacs.6b05475},
      url          = {https://juser.fz-juelich.de/record/820729},
}