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@ARTICLE{Kwon:875158,
      author       = {Kwon, Hanna and Basran, Jaswir and Devos, Juliette M. and
                      Suardíaz, Reynier and van der Kamp, Marc W. and Mulholland,
                      Adrian J. and Schrader, Tobias E. and Ostermann, Andreas and
                      Blakeley, Matthew P. and Moody, Peter C. E. and Raven, Emma
                      L.},
      title        = {{V}isualizing the protons in a metalloenzyme electron
                      proton transfer pathway},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {117},
      number       = {12},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2020-01848},
      pages        = {6484 - 6490},
      year         = {2020},
      abstract     = {In redox metalloenzymes, the process of electron transfer
                      often involves the concerted movement of a proton. These
                      processes are referred to as proton-coupled electron
                      transfer, and they underpin a wide variety of biological
                      processes, including respiration, energy conversion,
                      photosynthesis, and metalloenzyme catalysis. The mechanisms
                      of proton delivery are incompletely understood, in part due
                      to an absence of information on exact proton locations and
                      hydrogen bonding structures in a bona fide metalloenzyme
                      proton pathway. Here, we present a 2.1-Å neutron crystal
                      structure of the complex formed between a redox
                      metalloenzyme (ascorbate peroxidase) and its reducing
                      substrate (ascorbate). In the neutron structure of the
                      complex, the protonation states of the electron/proton donor
                      (ascorbate) and all of the residues involved in the
                      electron/proton transfer pathway are directly observed. This
                      information sheds light on possible proton movements during
                      heme-catalyzed oxygen activation, as well as on ascorbate
                      oxidation.},
      cin          = {JCNS-FRM-II / MLZ / JCNS-1},
      ddc          = {500},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6215 /
                      G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32152099},
      UT           = {WOS:000521821800034},
      doi          = {10.1073/pnas.1918936117},
      url          = {https://juser.fz-juelich.de/record/875158},
}