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@ARTICLE{Stadler:866225,
      author       = {Stadler, Andreas Maximilian and Schneidewind, Judith and
                      Zamponi, Michaela and Knieps-Grünhagen, Esther and Gholami,
                      Samira and Schwaneberg, Ulrich and Rivalta, Ivan and
                      Garavelli, Marco and Davari, Mehdi D. and Jaeger, Karl-Erich
                      and Krauss, Ulrich},
      title        = {{T}ernary {C}omplex {F}ormation and {P}hotoactivation of a
                      {P}hotoenzyme {R}esults in {A}ltered {P}rotein {D}ynamics},
      journal      = {The journal of physical chemistry / B B, Condensed matter,
                      materials, surfaces, interfaces $\&$ biophysical},
      volume       = {123},
      number       = {34},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2019-05391},
      pages        = {7372 - 7384},
      year         = {2019},
      abstract     = {The interplay between protein dynamics and catalysis
                      remains a fundamental question in enzymology. We here
                      investigate the ns-timescale dynamics of a light-dependent
                      NADPH:protochlorophyllide oxidoreductase (LPOR), a
                      photoenzyme crucial for chlorophyll synthesis. LPORs
                      catalyze the light-triggered trans addition of a hydride and
                      a proton across the C17═C18 double bond of the chlorophyll
                      precursor protochlorophyllide (Pchlide). Because of the lack
                      of an LPOR structure, the global structural and dynamic
                      consequences of LPOR/Pchlide/NADPH ternary complex formation
                      remain elusive. Moreover, photoactivation of LPORs by
                      low-light preillumination is controversially discussed as
                      unequivocal proof for this phenomenon is lacking. By
                      employing quasielastic neutron spectroscopy (QENS), we show
                      that the formation of the ternary holoprotein complex as
                      well as photoactivation lead to progressive rigidification
                      of the protein. These findings are supported by
                      thermostability measurements, which reveal different melting
                      behavior and thermostabilities for the apo- and holoprotein
                      ternary complexes. Molecular dynamics simulations in good
                      agreement with the experimental QENS results suggest that
                      the increased flexibility observed for the apoprotein stems
                      from structural fluctuations of the NADPH and Pchlide
                      substrate binding sites of the enzyme. On the basis of our
                      results, in conjunction with activity and stability
                      measurements, we provide independent proof for LPOR
                      photoactivation, defined as a process that modifies the
                      protein structure and dynamics, resulting in an increased
                      substrate turnover. Our findings advance the structural and
                      dynamic understanding of LPORs and provide a first link
                      between protein dynamics and catalysis for this enzyme
                      class.},
      cin          = {IMET / IBG-1 / ICS-1 / JCNS-1 / JCNS-FRM-II},
      ddc          = {530},
      cid          = {I:(DE-Juel1)IMET-20090612 / I:(DE-Juel1)IBG-1-20101118 /
                      I:(DE-Juel1)ICS-1-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218},
      pnm          = {581 - Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-581},
      experiment   = {EXP:(DE-MLZ)SPHERES-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31380636},
      UT           = {WOS:000484074500013},
      doi          = {10.1021/acs.jpcb.9b06608},
      url          = {https://juser.fz-juelich.de/record/866225},
}