% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Kalkan:594783,
      author       = {Kalkan, Ozlem and Kantamneni, Sravya and Brings, Lea and
                      Han, Huijong and Bean, Richard and Mancuso, Adrian and Koua,
                      Faisal H. M.},
      title        = {{H}eterologous expression, purification and structural
                      features of native {D}ictyostelium discoideum
                      dye-decolorizing peroxidase bound to a natively incorporated
                      heme},
      journal      = {Frontiers in Chemistry},
      volume       = {11},
      issn         = {2296-2646},
      address      = {Lausanne},
      publisher    = {Frontiers Media},
      reportid     = {PUBDB-2023-05960},
      pages        = {1220543},
      year         = {2023},
      abstract     = {The Dictyostelium discoideum dye-decolorizing peroxidase
                      (DdDyP) is a newly discovered peroxidase, which belongs to a
                      unique class of heme peroxidase family that lacks homology
                      to the known members of plant peroxidase superfamily. DdDyP
                      catalyzes the H$_2$O$_2$-dependent oxidation of a
                      wide-spectrum of substrates ranging from polycyclic dyes to
                      lignin biomass, holding promise for potential industrial and
                      biotechnological applications. To study the molecular
                      mechanism of DdDyP, highly pure and functional protein with
                      a natively incorporated heme is required, however, obtaining
                      a functional DyP-type peroxidase with a natively bound heme
                      is challenging and often requires addition of expensive
                      biosynthesis precursors. Alternatively, a heme in vitro
                      reconstitution approach followed by a chromatographic
                      purification step to remove the excess heme is often used.
                      Here, we show that expressing the DdDyP peroxidase in ×2 YT
                      enriched medium at low temperature (20°C), without adding
                      heme supplement or biosynthetic precursors, allows for a
                      correct native incorporation of heme into the apo-protein,
                      giving rise to a stable protein with a strong Soret peak at
                      402 nm. Further, we crystallized and determined the native
                      structure of DdDyP at a resolution of 1.95 Å, which
                      verifies the correct heme binding and its geometry. The
                      structural analysis also reveals a binding of two water
                      molecules at the distal site of heme plane bridging the
                      catalytic residues (Arg239 and Asp149) of the GXXDG motif to
                      the heme-Fe(III) via hydrogen bonds. Our results provide new
                      insights into the geometry of native DdDyP active site and
                      its implication on DyP catalysis.},
      cin          = {DOOR ; HAS-User / $XFEL_E1_SPB/SFX$ / $XFEL_E2_SEC$},
      ddc          = {540},
      cid          = {I:(DE-H253)HAS-User-20120731 /
                      $I:(DE-H253)XFEL_E1_SPB_SFX-20210408$ /
                      $I:(DE-H253)XFEL_E2_SEC-20210408$},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P11-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {37593106},
      UT           = {WOS:001049107300001},
      doi          = {10.3389/fchem.2023.1220543},
      url          = {https://bib-pubdb1.desy.de/record/594783},
}