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@ARTICLE{Hiromoto:87264,
      author       = {Hiromoto, Takashi and Ataka, Kenichi and Pilak, Oliver and
                      Vogt, S. and Salamone Stagni, Marco and Meyer-Klaucke, W.
                      and Warkentin, Eberhard and Thauer, Rudolf K. and Shima,
                      Seigo and Ermler, U. and DESY},
      title        = {{T}he {C}rystal {S}tructure of {C}176{A} {M}utated
                      [{F}e]-{H}ydrogenase {S}uggests an {A}cyl-{I}ron {L}igation
                      in the {A}ctive {S}ite {I}ron {C}omplex},
      journal      = {FEBS letters},
      volume       = {583},
      issn         = {0014-5793},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PHPPUBDB-8575},
      pages        = {585-590},
      year         = {2009},
      note         = {(c) Federation of European Biochemical Societies. Post
                      referee full text in progress (embargo 1 year from 20 JAN
                      2009).},
      abstract     = {[Fe]-hydrogenase is one of three types of enzymes known to
                      activate H(2). Crystal structure analysis recently revealed
                      that its active site iron is ligated square-pyramidally by
                      Cys176-sulfur, two CO, an "unknown" ligand and the
                      sp(2)-hybridized nitrogen of a unique
                      iron-guanylylpyridinol-cofactor. We report here on the
                      structure of the C176A mutated enzyme crystallized in the
                      presence of dithiothreitol (DTT). It suggests an iron center
                      octahedrally coordinated by one DTT-sulfur and one
                      DTT-oxygen, two CO, the 2-pyridinol's nitrogen and the
                      2-pyridinol's 6-formylmethyl group in an acyl-iron ligation.
                      This result led to a re-interpretation of the iron ligation
                      in the wild-type.},
      keywords     = {Adenine: metabolism / Catalytic Domain / Crystallography,
                      X-Ray / Cytosine: metabolism / Holoenzymes: chemistry /
                      Holoenzymes: genetics / Holoenzymes: metabolism /
                      Hydrogenase: chemistry / Hydrogenase: genetics /
                      Hydrogenase: metabolism / Iron: chemistry / Iron: metabolism
                      / Iron-Sulfur Proteins: chemistry / Iron-Sulfur Proteins:
                      genetics / Iron-Sulfur Proteins: metabolism /
                      Methanococcales: enzymology / Methanococcales: genetics /
                      Mutation: genetics / Protein Structure, Quaternary /
                      Holoenzymes (NLM Chemicals) / Iron-Sulfur Proteins (NLM
                      Chemicals) / Cytosine (NLM Chemicals) / Adenine (NLM
                      Chemicals) / Iron (NLM Chemicals) / iron hydrogenase (NLM
                      Chemicals) / Hydrogenase (NLM Chemicals)},
      cin          = {HASYLAB(-2012) / EMBL(-2012)},
      ddc          = {570},
      cid          = {$I:(DE-H253)HASYLAB_-2012_-20130307$ /
                      $I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {FS Beamline without reference (POF1-550)},
      pid          = {G:(DE-H253)POF1-No-Ref-20130405},
      experiment   = {EXP:(DE-H253)Unknown-BL-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19162018},
      UT           = {WOS:000263603600014},
      doi          = {10.1016/j.febslet.2009.01.017},
      url          = {https://bib-pubdb1.desy.de/record/87264},
}