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@ARTICLE{Akola:51046,
      author       = {Akola, J. and Jones, R. O.},
      title        = {{D}ensity functional calculations of {ATP} systems {II}:
                      {ATP} hydrolysis at the active site of actin},
      journal      = {The journal of physical chemistry / B},
      volume       = {110},
      issn         = {1520-6106},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {PreJuSER-51046},
      pages        = {8121 - 8129},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The hydrolysis of adenosine 5'-triphosphate (ATP) at the
                      active site of actin has been studied using density
                      functional calculations. The active site is modeled by the
                      triphosphate tail of ATP, an Mg cation, surrounding water
                      molecules, and the nearby protein residues. Four reaction
                      paths have been followed by constraining coordinates that
                      allow phosphate stretching, nucleophilic attack of the
                      catalytic water, and OH(-) formation via water
                      deprotonation. The lowest-energy barrier (21.0 kcal/mol) is
                      obtained for a dissociative reaction where the terminal
                      phosphate breaks on approaching the catalytic water,
                      followed by proton release via a proton wire mechanism. A
                      higher barrier (39.6 kcal/mol) results for an associative
                      reaction path where OH(-) is formed first, with a
                      pentacoordinated phosphorus atom (P-O distances 2.1 A).
                      Stretching the terminal bridging P-O bond results in bond
                      rupture at 2.8 A with an energy barrier of 28.8 kcal/mol.
                      The residues Gln137 and His161 are not important in the
                      reactions, but insight into their roles in vivo has been
                      obtained. The favored coordination of the end products
                      H(2)PO(4)(-) and ADP(3-) includes a hydrogen bond and an
                      O-Mg-O bridge between the phosphates as well as a hydrogen
                      bond between H(2)PO(4)(-) and the Ser14 side chain. The
                      total energy is 2.1 kcal/mol lower than in the initial
                      reactants. Classical simulations of ATP- and ADP.P(i)-actin
                      show few hydrolysis-induced differences in the protein
                      structure, indicating that phosphate migration is necessary
                      for a change in conformation.},
      keywords     = {Actins: chemistry / Adenosine Triphosphate: chemistry /
                      Binding Sites / Hydrogen Bonding / Hydrolysis / Models,
                      Molecular / Saccharomyces cerevisiae: chemistry / Actins
                      (NLM Chemicals) / Adenosine Triphosphate (NLM Chemicals) / J
                      (WoSType)},
      cin          = {IFF-TH-I},
      ddc          = {530},
      cid          = {I:(DE-Juel1)VDB30},
      pnm          = {Kondensierte Materie},
      pid          = {G:(DE-Juel1)FUEK414},
      shelfmark    = {Chemistry, Physical},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16610915},
      UT           = {WOS:000236992100069},
      doi          = {10.1021/jp054921d},
      url          = {https://juser.fz-juelich.de/record/51046},
}