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@ARTICLE{Jckering:1031817,
      author       = {Jäckering, Anna and van der Kamp, Marc and Strodel, Birgit
                      and Zinovjev, Kirill},
      title        = {{I}nfluence of {W}obbling {T}ryptophan and {M}utations on
                      {PET} {D}egradation {E}xplored by {QM}/{MM} {F}ree {E}nergy
                      {C}alculations},
      journal      = {Journal of chemical information and modeling},
      volume       = {11},
      issn         = {1549-9596},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2024-05836},
      pages        = {acs.jcim.4c00776},
      year         = {2024},
      abstract     = {ABSTRACT: Plastic-degrading enzymes, particularly
                      poly(ethylene terephthalate)(PET) hydrolases, have garnered
                      significant attention in recent years aspotential
                      eco-friendly solutions for recycling plastic waste. However,
                      understandingof their PET-degrading activity and influencing
                      factors remainsincomplete, impeding the development of
                      uniform approaches for enhancingPET hydrolases for
                      industrial applications. A key aspect of PET
                      hydrolaseengineering is optimizing the PET-hydrolysis
                      reaction by lowering the associatedfree energy barrier.
                      However, inconsistent findings have complicated these
                      efforts.Therefore, our goal is to elucidate various aspects
                      of enzymatic PET degradationby means of quantum
                      mechanics/molecular mechanics (QM/MM) reactionsimulations
                      and analysis, focusing on the initial reaction step,
                      acylation, in twothermophilic PET hydrolases, LCC and
                      PES-H1, along with their highly active variants, LCCIG and
                      PES-H1FY. Our findingshighlight the impact of semiempirical
                      QM methods on proton transfer energies, affecting the
                      distinction between a two-step reactioninvolving a
                      metastable tetrahedral intermediate and a one-step reaction.
                      Moreover, we uncovered a concerted conformational
                      changeinvolving the orientation of the PET benzene ring,
                      altering its interaction with the side-chain of the
                      “wobbling” tryptophan from Tstackingto parallel π−π
                      interactions, a phenomenon overlooked in prior research. Our
                      study thus enhances the understanding of theacylation
                      mechanism of PET hydrolases, in particular by characterizing
                      it for the first time for the promising PES-H1FY using QM/MM
                      simulations. It also provides insights into selecting a
                      suitable QM method and a reaction coordinate, valuable for
                      future studieson PET degradation processes.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {39344272},
      UT           = {WOS:001325651400001},
      doi          = {10.1021/acs.jcim.4c00776},
      url          = {https://juser.fz-juelich.de/record/1031817},
}