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@ARTICLE{Kwon:826420,
      author       = {Kwon, Hanna and Basran, Jaswir and Casadei, Cecilia M. and
                      Fielding, Alistair J. and Schrader, Tobias E. and Ostermann,
                      Andreas and Devos, Juliette M. and Aller, Pierre and
                      Blakeley, Matthew P. and Moody, Peter C. E. and Raven, Emma
                      L.},
      title        = {{D}irect visualization of a {F}e({IV})–{OH} intermediate
                      in a heme enzyme},
      journal      = {Nature Communications},
      volume       = {7},
      issn         = {2041-1723},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2017-00648},
      pages        = {13445 -},
      year         = {2016},
      abstract     = {Catalytic heme enzymes carry out a wide range of oxidations
                      in biology. They have in common a mechanism that requires
                      formation of highly oxidized ferryl intermediates. It is
                      these ferryl intermediates that provide the catalytic engine
                      to drive the biological activity. Unravelling the nature of
                      the ferryl species is of fundamental and widespread
                      importance. The essential question is whether the ferryl is
                      best described as a Fe(IV)=O or a Fe(IV)–OH species, but
                      previous spectroscopic and X-ray crystallographic studies
                      have not been able to unambiguously differentiate between
                      the two species. Here we use a different approach. We report
                      a neutron crystal structure of the ferryl intermediate in
                      Compound II of a heme peroxidase; the structure allows the
                      protonation states of the ferryl heme to be directly
                      observed. This, together with pre-steady state kinetic
                      analyses, electron paramagnetic resonance spectroscopy and
                      single crystal X-ray fluorescence, identifies a Fe(IV)–OH
                      species as the reactive intermediate. The structure
                      establishes a precedent for the formation of Fe(IV)–OH in
                      a peroxidase.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {500},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000388990900001},
      pubmed       = {pmid:27897163},
      doi          = {10.1038/ncomms13445},
      url          = {https://juser.fz-juelich.de/record/826420},
}