% 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”.

@PHDTHESIS{kraus:638201,
      author       = {kraus, yasemine},
      title        = {{B}iophysikalische {U}ntersuchung von an
                      {B}iotransformationbeteiligten {F}lavinmonooxygenasen},
      school       = {Christian - Albrechts - Universität zu Kiel},
      type         = {Dissertation},
      reportid     = {PUBDB-2025-04019},
      pages        = {1-345},
      year         = {2025},
      note         = {Dissertation, Christian - Albrechts - Universität zu Kiel,
                      2025},
      abstract     = {This work deals with the expression, purification,
                      characterization, and crystallization of ΔhFMO5,a variant
                      of the human flavin-dependent monooxygenase 5 (hFMO5)
                      without transmembraneregion. This modification enables the
                      expression and purification of soluble protein
                      withoutaddition of detergent, resulting in the isolation of
                      active protein saturated with FAD. Theaggregation prone
                      ΔhFMO5 was successfully expressed in a fermenter using the
                      strain E. coliRosetta 2 (DE3) pLysS, lysed by enzymatic cell
                      disruption and purified through affinity and sizeexclusion
                      chromatography. Characterization of ΔhFMO5 via mass
                      photometry reveals that insolution there is present a
                      mixture of different oligomeric states, with the tetrameric
                      form beingpredominant. The catalytic cycle of ΔhFMO5
                      includes an uncoupled metabolic pathway, in whichNADPH is
                      consumed to regenerate the FAD cofactor without substrate
                      turnover, leading to theformation of hydrogen peroxide.
                      Iterative modeling of the reaction kinetics of
                      ΔhFMO5demonstrates that substrate metabolism as a
                      second-order reaction proceeds more slowlycompared to the
                      uncoupled reaction. Activity measurements show that the
                      conversion ofphenylacetone to benzyl acetate is catalyzed by
                      ΔhFMO5 with a turnover rate of 5.1 $\%.$ N-acetylserotonin
                      was identified as a potential endogenous substrate playing a
                      role in the productionof melatonin and serotonin.},
      cin          = {EMBL-User},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)11},
      url          = {https://bib-pubdb1.desy.de/record/638201},
}