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@ARTICLE{Chernomor:884241,
      author       = {Chernomor, Olga and Peters, Lena and Schneidewind, Judith
                      and Loeschcke, Anita and Knieps-Grünhagen, Esther and
                      Schmitz, Fabian and von Lieres, Eric and Kutta, Roger Jan
                      and Svensson, Vera and Jaeger, Karl-Erich and Drepper,
                      Thomas and von Haeseler, Arndt and Krauss, Ulrich},
      title        = {{C}omplex evolution of light-dependent protochlorophyllide
                      oxidoreductases in aerobic anoxygenic phototrophs: origin,
                      phylogeny and function},
      journal      = {Molecular biology and evolution},
      volume       = {38},
      number       = {3},
      issn         = {1537-1719},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {FZJ-2020-03140},
      pages        = {819-837},
      year         = {2021},
      abstract     = {Light-dependent and dark-operative protochlorophyllide
                      oxidoreductases (LPORs and DPORs) are evolutionary and
                      structurally distinct enzymes that are essential for the
                      synthesis of (bacterio)chlorophyll, the primary pigment
                      needed for both anoxygenic and oxygenic photosynthesis. In
                      contrast to the long-held hypothesis that LPORs are only
                      present in oxygenic phototrophs, we recently identified a
                      functional LPOR in the aerobic anoxygenic phototrophic
                      bacterium (AAPB) Dinoroseobacter shibae, and attributed its
                      presence to a single horizontal gene transfer (HGT) event
                      from cyanobacteria. Here, we provide evidence for the more
                      widespread presence of genuine LPOR enzymes in AAPBs. An
                      exhaustive bioinformatics search identified 36 putative
                      LPORs outside of oxygenic phototrophic bacteria
                      (cyanobacteria) with the majority being AAPBs. Using in
                      vitro and in vivo assays, we show that the large majority of
                      the tested AAPB enzymes are genuine LPORs. Solution
                      structural analyses, performed for two of the AAPB LPORs,
                      revealed a globally conserved structure when compared to a
                      well-characterized cyanobacterial LPOR. Phylogenetic
                      analyses suggest that LPORs were transferred not only from
                      cyanobacteria, but also subsequently between proteobacteria
                      and from proteobacteria to Gemmatimonadetes. Our study thus
                      provides another interesting example for the complex
                      evolutionary processes that govern the evolution of
                      bacteria, involving multiple HGT events that likely occurred
                      at different time points and involved different donors.},
      cin          = {IBG-1 / IMET},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBG-1-20101118 / I:(DE-Juel1)IMET-20090612},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217)},
      pid          = {G:(DE-HGF)POF4-2171},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32931580},
      UT           = {WOS:000651826600007},
      doi          = {10.1093/molbev/msaa234},
      url          = {https://juser.fz-juelich.de/record/884241},
}