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@ARTICLE{Zuo:894686,
      author       = {Zuo, Ke and Marjault, Henri-Baptiste and Bren, Kara L. and
                      Rossetti, Giulia and Nechushtai, Rachel and Carloni, Paolo},
      title        = {{T}he two redox states of the human {NEET} proteins’
                      [2{F}e–2{S}] clusters},
      journal      = {Journal of biological inorganic chemistry},
      volume       = {26},
      issn         = {1432-1327},
      address      = {New York},
      publisher    = {Springer},
      reportid     = {FZJ-2021-03348},
      pages        = {763–774},
      year         = {2021},
      abstract     = {The NEET proteins constitute a unique class of [2Fe–2S]
                      proteins. The metal ions bind to three cysteines and one
                      histidine. The proteins’ clusters exist in two redox
                      states; the oxidized protein (containing two FeIII ions) can
                      transfer the cluster to apo-acceptor protein(s), while the
                      reduced form (containing one ferrous ion) remains bound to
                      the protein frame. Here, we perform in silico and in vitro
                      studies on human NEET proteins in both reduced and oxidized
                      forms. Quantum chemical calculations on all available human
                      NEET proteins structures suggest that reducing the cluster
                      weakens the Fe–NHis and Fe–SCys bonds, similar to what
                      is seen in other Fe–S proteins (e.g., ferredoxin and
                      Rieske protein). We further show that the extra electron in
                      the [2Fe–2S]+ clusters of one of the NEET proteins (mNT)
                      is localized on the His-bound iron ion, consistently with
                      our previous spectroscopic studies. Kinetic measurements
                      demonstrate that the mNT [2Fe–2S]+ is released only by an
                      increase in temperature. Thus, the reduced state of human
                      NEET proteins [2Fe–2S] cluster is kinetically inert. This
                      previously unrecognized kinetic inertness of the reduced
                      state, along with the reactivity of the oxidized state, is
                      unique across all [2Fe–2S] proteins. Finally, using a
                      coevolutionary analysis, along with molecular dynamics
                      simulations, we provide insight on the observed allostery
                      between the loop L2 and the cluster region. Specifically, we
                      show that W75, R76, K78, K79, F82 and G85 in the latter
                      region share similar allosteric characteristics in both
                      redox states.},
      cin          = {IAS-5 / INM-9 / JSC},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121 /
                      I:(DE-Juel1)JSC-20090406},
      pnm          = {5252 - Brain Dysfunction and Plasticity (POF4-525) / 5111 -
                      Domain-Specific Simulation $\&$ Data Life Cycle Labs (SDLs)
                      and Research Groups (POF4-511)},
      pid          = {G:(DE-HGF)POF4-5252 / G:(DE-HGF)POF4-5111},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34453614},
      UT           = {WOS:000690718000002},
      doi          = {10.1007/s00775-021-01890-8},
      url          = {https://juser.fz-juelich.de/record/894686},
}