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@ARTICLE{Borshchevskiy:279385,
      author       = {Borshchevskiy, Valentin and Round, Ekaterina and Bertsova,
                      Yulia and Polovinkin, Vitaly and Gushchin, Ivan and
                      Ishchenko, Andrii and Kovalev, Kirill and Mishin, Alexey and
                      Kachalova, Galina and Popov, Alexander and Bogachev,
                      Alexander and Gordeliy, Valentin},
      title        = {{S}tructural and functional investigation of flavin binding
                      center of the {N}qr{C} subunit of sodium-translocating
                      {NADH}:{Q}uinone oxidoreductase from {V}ibrio harveyi},
      journal      = {PLoS one},
      volume       = {10},
      number       = {3},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2015-07397},
      pages        = {e0118548},
      year         = {2015},
      abstract     = {Na+-translocating NADH:quinone oxidoreductase (NQR) is a
                      redox-driven sodium pump operating in the respiratory chain
                      of various bacteria, including pathogenic species. The
                      enzyme has a unique set of redox active prosthetic groups,
                      which includes two covalently bound flavin mononucleotide
                      (FMN) residues attached to threonine residues in subunits
                      NqrB and NqrC. The reason of FMN covalent bonding in the
                      subunits has not been established yet. In the current work,
                      binding of free FMN to the apo-form of NqrC from Vibrio
                      harveyi was studied showing very low affinity of NqrC to FMN
                      in the absence of its covalent bonding. To study structural
                      aspects of flavin binding in NqrC, its holo-form was
                      crystallized and its 3D structure was solved at 1.56 Å
                      resolution. It was found that the isoalloxazine moiety of
                      the FMN residue is buried in a hydrophobic cavity and that
                      its pyrimidine ring is squeezed between hydrophobic amino
                      acid residues while its benzene ring is extended from the
                      protein surroundings. This structure of the flavin-binding
                      pocket appears to provide flexibility of the benzene ring,
                      which can help the FMN residue to take the bended
                      conformation and thus to stabilize the one-electron reduced
                      form of the prosthetic group. These properties may also lead
                      to relatively weak noncovalent binding of the flavin. This
                      fact along with periplasmic location of the FMN-binding
                      domains in the vast majority of NqrC-like proteins may
                      explain the necessity of the covalent bonding of this
                      prosthetic group to prevent its loss to the external
                      medium.},
      cin          = {ICS-6},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000350314700037},
      pubmed       = {pmid:25734798},
      doi          = {10.1371/journal.pone.0118548},
      url          = {https://juser.fz-juelich.de/record/279385},
}