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@ARTICLE{Syllwasschy:889869,
      author       = {Syllwasschy, Benjamin Franz and Beck, Maximilian Steve and
                      Družeta, Ivona and Hopp, Marie-Thérèse and Ramoji,
                      Anuradha and Neugebauer, Ute and Nozinovic, Senada and
                      Menche, Dirk and Willbold, Dieter and Ohlenschläger, Oliver
                      and Kühl, Toni and Imhof, Diana},
      title        = {{H}igh-affinity binding and catalytic activity of
                      {H}is/{T}yr-based sequences: {E}xtending heme-regulatory
                      motifs beyond {CP}},
      journal      = {Biochimica et biophysica acta / General subjects},
      volume       = {1864},
      number       = {7},
      issn         = {0304-4165},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2021-00477},
      pages        = {129603 -},
      year         = {2020},
      note         = {Kein Post-print verfügbar},
      abstract     = {Background $\&$ motivationPeptides and proteins can
                      interact with heme through His, Tyr, or Cys in
                      heme-regulatory motifs (HRMs). The Cys-Pro dipeptide is a
                      well investigated HRM, but for His and Tyr such a distinct
                      motif is currently unknown. In addition, many heme-peptide
                      complexes, such as heme-amyloid β, can display a
                      peroxidase-like activity, albeit there is little
                      understanding of how the local primary and secondary
                      coordination environment influences catalytic activity. We
                      thus systematically evaluated a series of His- and Tyr-based
                      peptides to identify sequence features for high-affinity
                      heme binding and their impact on the catalytic activity of
                      heme.MethodsWe employed solid-phase peptide synthesis to
                      produce 58 nonapeptides, which were investigated by UV/vis,
                      resonance Raman, and 2D NMR spectroscopy. A chromogenic
                      assay was used to determine the catalytic activity of the
                      heme-peptide complexes.ResultsHeme-binding affinity and
                      binding mode were found to be dependent on the coordinating
                      amino acid and spacer length between multiple potential
                      coordination sites in a motif. In particular, HXH and HXXXH
                      motifs showed strong heme binding. Analysis of the
                      peroxidase-like activity revealed that some of these
                      peptides and also HXXXY motifs enhance the catalytic
                      activity of heme significantly.ConclusionsWe identify HXH,
                      HXXXH, and HXXXY as potential new HRMs with functional
                      properties. Several peptides displayed a strikingly high
                      peroxidase-like activity.General significanceThe
                      identification of HRMs allows to discover yet unknown
                      heme-regulated proteins, and consequently, enhances our
                      current understanding of pathologies involving labile heme.},
      cin          = {IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32234408},
      UT           = {WOS:000536132200008},
      doi          = {10.1016/j.bbagen.2020.129603},
      url          = {https://juser.fz-juelich.de/record/889869},
}