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@ARTICLE{Sushko:904321,
      author       = {Sushko, Tatsiana and Kavaleuski, Anton and Grabovec, Irina
                      and Kavaleuskaya, Anna and Vakhrameev, Daniil and
                      Bukhdruker, Sergey and Marin, Egor and Kuzikov, Alexey and
                      Shumyantseva, Victoria and Masamrekh, Rami and Tsumoto,
                      Kouhei and Borshchevskiy, Valentin and Strushkevich,
                      Natallia and Gilep, Andrei},
      title        = {{A} new twist of rubredoxin function in {M}. tuberculosis},
      journal      = {Bioorganic chemistry},
      volume       = {109},
      issn         = {0045-2068},
      address      = {San Diego, Calif.},
      publisher    = {Elsevier},
      reportid     = {FZJ-2021-05891},
      pages        = {104721 -},
      year         = {2021},
      abstract     = {Electron transfer mediated by metalloproteins drives many
                      biological processes. Rubredoxins are a ubiquitous [1Fe-0S]
                      class of electron carriers that play an important role in
                      bacterial adaptation to changing environmental conditions.
                      In Mycobacterium tuberculosis, oxidative and acidic stresses
                      as well as iron starvation induce rubredoxins expression.
                      However, their functions during M. tuberculosis infection
                      are unknown. In the present work, we show that rubredoxin B
                      (RubB) is able to efficiently shuttle electrons from cognate
                      reductases, FprA and FdR to support catalytic activity of
                      cytochrome P450s, CYP124, CYP125, and CYP142, which are
                      important for bacterial viability and pathogenicity. We
                      solved the crystal structure of RubB and characterized the
                      interaction between RubB and CYPs using site-directed
                      mutagenesis. Mutations that not only neutralize single
                      charge but also change the specific residues on the surface
                      of RubB did not dramatically decrease activity of studied
                      CYPs. Together with isothermal calorimetry (ITC)
                      experiments, the obtained results suggest that interactions
                      are transient and not highly specific. The redox potential
                      of RubB is −264 mV vs. Ag/AgCl and the measured extinction
                      coefficients are 9931 M−1cm−1 and 8371 M−1cm−1 at
                      380 nm and 490 nm, respectively. Characteristic parameters
                      of RubB along with the discovered function might be useful
                      for biotechnological applications. Our findings suggest that
                      a switch from ferredoxins to rubredoxins might be crucial
                      for M. tuberculosis to support CYPs activity during the
                      infection.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33618255},
      UT           = {WOS:000636139600003},
      doi          = {10.1016/j.bioorg.2021.104721},
      url          = {https://juser.fz-juelich.de/record/904321},
}