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@ARTICLE{Kokorin:904482,
      author       = {Kokorin, Arsenij and Parshin, Pavel D. and Bakkes, Patrick
                      J. and Pometun, Anastasia A. and Tishkov, Vladimir I. and
                      Urlacher, Vlada B.},
      title        = {{G}enetic fusion of {P}450 {BM}3 and formate dehydrogenase
                      towards self-sufficient biocatalysts with enhanced activity},
      journal      = {Scientific reports},
      volume       = {11},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2021-06052},
      pages        = {21706},
      year         = {2021},
      abstract     = {Fusion of multiple enzymes to multifunctional constructs
                      has been recognized as a viable strategy to improve
                      enzymatic properties at various levels such as stability,
                      activity and handling. In this study, the genes coding for
                      cytochrome P450 BM3 from B. megaterium and formate
                      dehydrogenase from Pseudomonas sp. were fused to enable both
                      substrate oxidation catalyzed by P450 BM3 and continuous
                      cofactor regeneration by formate dehydrogenase within one
                      construct. The order of the genes in the fusion as well as
                      the linkers that bridge the enzymes were varied. The
                      resulting constructs were compared to individual enzymes
                      regarding substrate conversion, stability and kinetic
                      parameters to examine whether fusion led to any substantial
                      improvements of enzymatic properties. Most noticeably, an
                      activity increase of up to threefold was observed for the
                      fusion constructs with various substrates which were partly
                      attributed to the increased diflavin reductase activity of
                      the P450 BM3. We suggest that P450 BM3 undergoes
                      conformational changes upon fusion which resulted in altered
                      properties, however, no NADPH channeling was detected for
                      the fusion constructs.},
      cin          = {IBG-1},
      ddc          = {600},
      cid          = {I:(DE-Juel1)IBG-1-20101118},
      pnm          = {2172 - Utilization of renewable carbon and energy sources
                      and engineering of ecosystem functions (POF4-217)},
      pid          = {G:(DE-HGF)POF4-2172},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34737365},
      UT           = {WOS:000714702000001},
      doi          = {10.1038/s41598-021-00957-5},
      url          = {https://juser.fz-juelich.de/record/904482},
}