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@ARTICLE{Kachalova:143955,
      author       = {Kachalova, G. S. and Shosheva, A. C. and Bourenkov, G. P.
                      and Donchev, A. A. and Dimitrov, M. I. and Bartunik, H. D.
                      and DESY},
      title        = {{S}tructural comparison of the poplar plastocyanin isoforms
                      {PC}a and {PC}b sheds new light on the role of the copper
                      site geometry in interactions with redox partners in
                      oxygenic photosynthesis},
      journal      = {Journal of inorganic biochemistry},
      volume       = {115},
      issn         = {0162-0134},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PHPPUBDB-25674},
      pages        = {174-181},
      year         = {2012},
      abstract     = {Plastocyanin (PC) from poplar leaves is present in two
                      isoforms, PCa and PCb, which differ in sequence by amino
                      acid replacements at locations remote from the copper center
                      and simultaneously act in the photosynthetic
                      electron-transport chain. We describe ultra-high resolution
                      structures of PCa and high-resolution structures of PCb,
                      both under oxidizing and reducing conditions at pH 4, 6 and
                      8. The docking on cytochrome f and photosystem I,
                      respectively, has been modeled for both isoforms. PCa and
                      PCb exhibit closely similar overall and active-site
                      structures, except for a difference in the relative
                      orientation of the acidic patches. The isoforms exhibit
                      substantial differences in the dependence of the reduced
                      (Cu(I)) geometry on pH. In PCa, the decrease in pH causes a
                      gradual dissociation of His87 from Cu(I) at low pH, probably
                      adopting a neutral tautomeric state. In PCb, the histidine
                      remains covalently bound to Cu(I) and may adopt a doubly
                      protonated state at low pH. The fact that both isoforms have
                      similar although not identical functions in photosynthetic
                      electron flows suggests that the His87 imidazole does not
                      play a crucial role for the pathway of electron transport
                      from cytochrome f to oxidized PC.},
      keywords     = {Copper: chemistry / Copper: metabolism / Cytochromes f:
                      chemistry / Cytochromes f: metabolism / Hydrogen-Ion
                      Concentration / Oxidation-Reduction / Photosynthesis:
                      physiology / Photosystem I Protein Complex: chemistry /
                      Photosystem I Protein Complex: metabolism / Plastocyanin:
                      chemistry / Plastocyanin: metabolism / Populus: chemistry /
                      Populus: metabolism / Protein Isoforms: chemistry / Protein
                      Isoforms: metabolism / Photosystem I Protein Complex (NLM
                      Chemicals) / Protein Isoforms (NLM Chemicals) / Copper (NLM
                      Chemicals) / Plastocyanin (NLM Chemicals) / Cytochromes f
                      (NLM Chemicals)},
      cin          = {HASYLAB},
      ddc          = {540},
      cid          = {$I:(DE-H253)HASYLAB_-2012_-20130307$},
      pnm          = {DORIS Beamline BW6 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-BW6-20130405},
      experiment   = {EXP:(DE-H253)D-BW6-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22883960},
      UT           = {WOS:000309990500023},
      doi          = {10.1016/j.jinorgbio.2012.07.015},
      url          = {https://bib-pubdb1.desy.de/record/143955},
}