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@ARTICLE{Mazzei:1018321,
      author       = {Mazzei, Luca and Paul, Arundhati and Cianci, Michele and
                      Devodier, Marta and Mandelli, Davide and Carloni, Paolo and
                      Ciurli, Stefano},
      title        = {{K}inetic and structural details of urease inactivation by
                      thiuram disulphides},
      journal      = {Journal of inorganic biochemistry},
      volume       = {250},
      issn         = {0162-0134},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2023-04706},
      pages        = {112398 -},
      year         = {2024},
      abstract     = {This paper reports on the molecular details of the
                      reactivity of urease, a nickel-dependent enzyme that
                      catalyses the last step of organic nitrogen mineralization,
                      with thiuram disulphides, a class of molecules known to
                      inac- tivate the enzyme with high efficacy but for which the
                      mechanism of action had not been yet established. IC50
                      values of tetramethylthiuram disulphide (TMTD or Thiram) and
                      tetraethylthiuram disulphide (TETD or Disul- firam) in the
                      low micromolar range were determined for plant and bacterial
                      ureases. The X-ray crystal structure of Sporosarcina
                      pasteurii urease inactivated by Thiram, determined at 1.68
                      Å resolution, revealed the presence of a covalent
                      modification of the catalytically essential cysteine
                      residue. This is located on the flexible flap that modulates
                      the size of the active site channel and cavity. Formation of
                      a Cys-S-S-C(S)-N(CH3)2 functionality responsible for enzyme
                      inactivation was observed. Quantum-mechanical calculations
                      carried out to rationalise the large reactivity of the
                      active site cysteine support the view that a conserved
                      histidine residue, adjacent to the cysteine in the active
                      site flap, modulates the charge and electron density along
                      the thiol S–H bond by shifting electrons towards the
                      sulphur atom and rendering the thiol proton more reactive.
                      We speculate that this proton could be transferred to the
                      nickel-coordinated urea amide group to yield a molecule of
                      ammonia from the generated Curea-NH3+ functionality during
                      catalysis.},
      cin          = {IAS-5 / INM-9},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {37879152},
      UT           = {WOS:001104731700001},
      doi          = {10.1016/j.jinorgbio.2023.112398},
      url          = {https://juser.fz-juelich.de/record/1018321},
}