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@ARTICLE{Bolton:1024817,
      author       = {Bolton, Rachel and Machelett, Moritz M. and Stubbs, Jack
                      and Axford, Danny and Caramello, Nicolas and Catapano,
                      Lucrezia and Malý, Martin and Rodrigues, Matthew J. and
                      Cordery, Charlotte and Tizzard, Graham J. and MacMillan,
                      Fraser and Engilberge, Sylvain and von Stetten, David and
                      Tosha, Takehiko and Sugimoto, Hiroshi and Worrall, Jonathan
                      A. R. and Webb, Jeremy S. and Zubkov, Mike and Coles, Simon
                      and Mathieu, Eric and Steiner, Roberto A. and Murshudov,
                      Garib and Schrader, Tobias E. and Orville, Allen M. and
                      Royant, Antoine and Evans, Gwyndaf and Hough, Michael A. and
                      Owen, Robin L. and Tews, Ivo},
      title        = {{A} redox switch allows binding of {F}e({II}) and
                      {F}e({III}) ions in the cyanobacterial iron-binding protein
                      {F}ut{A} from {P}rochlorococcus},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {121},
      number       = {12},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2024-02483},
      pages        = {e2308478121},
      year         = {2024},
      abstract     = {The marine cyanobacterium Prochlorococcus is a main
                      contributor to global photosynthesis, whilst being limited
                      by iron availability. Cyanobacterial genomes generally
                      encode two different types of FutA iron-binding proteins:
                      periplasmic FutA2 ABC transporter subunits bind Fe(III),
                      while cytosolic FutA1 binds Fe(II). Owing to their small
                      size and their economized genome Prochlorococcus ecotypes
                      typically possess a single futA gene. How the encoded FutA
                      protein might bind different Fe oxidation states was
                      previously unknown. Here, we use structural biology
                      techniques at room temperature to probe the dynamic behavior
                      of FutA. Neutron diffraction confirmed four negatively
                      charged tyrosinates, that together with a neutral water
                      molecule coordinate iron in trigonal bipyramidal geometry.
                      Positioning of the positively charged Arg103 side chain in
                      the second coordination shell yields an overall
                      charge-neutral Fe(III) binding state in structures
                      determined by neutron diffraction and serial femtosecond
                      crystallography. Conventional rotation X-ray crystallography
                      using a home source revealed X-ray-induced photoreduction of
                      the iron center with observation of the Fe(II) binding
                      state; here, an additional positioning of the Arg203 side
                      chain in the second coordination shell maintained an overall
                      charge neutral Fe(II) binding site. Dose series using serial
                      synchrotron crystallography and an XFEL X-ray pump–probe
                      approach capture the transition between Fe(III) and Fe(II)
                      states, revealing how Arg203 operates as a switch to
                      accommodate the different iron oxidation states. This
                      switching ability of the Prochlorococcus FutA protein may
                      reflect ecological adaptation by genome streamlining and
                      loss of specialized FutA proteins.},
      cin          = {JCNS-FRM-II / JCNS-4 / MLZ},
      ddc          = {500},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-4-20201012 / I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (FZJ)
                      (POF4-6G4) / 632 - Materials – Quantum, Complex and
                      Functional Materials (POF4-632)},
      pid          = {G:(DE-HGF)POF4-6G4 / G:(DE-HGF)POF4-632},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {38489389},
      UT           = {WOS:001206418700003},
      doi          = {10.1073/pnas.2308478121},
      url          = {https://juser.fz-juelich.de/record/1024817},
}