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@ARTICLE{Caserta:481804,
      author       = {Caserta, Giorgio and Hartmann, Sven and van Stappen, Casey
                      and Karafoulidi Retsou, Chara and Lorent, Christian and
                      Yelin, Stefan and Keck, Matthias and Schoknecht, Janna and
                      Sergueev, Ilya and Yoda, Yoshitaka and Hildebrandt, Peter
                      and Limberg, Christian and DeBeer, Serena and Zebger, Ingo
                      and Frielingsdorf, Stefan and Lenz, Oliver},
      title        = {{A}ctive site assembly of [{N}i{F}e]-hydrogenase
                      scrutinized on the basis of purified maturation
                      intermediates},
      reportid     = {PUBDB-2022-04572},
      year         = {2022},
      note         = {Funding:Einstein Foundation Berlin: grant number
                      EVF-2016-277;SPP 1927 “Iron Sulfur for Life”: grants:
                      DE1877/1-1 and 311062227;Use of the Stanford Synchrotron
                      Radiation Lightsource, SLAC National Accelerator Laboratory,
                      was supported by the U.S. Department of Energy, Office of
                      Science, Office of Basic Energy Sciences under Contract No.
                      DE-AC02-76SF00515},
      abstract     = {[NiFe]-hydrogenases are biotechnologically relevant enzymes
                      catalyzing the reversible splitting of H$_2$ into 2 e$^- $
                      and 2 H$^+$ under ambient conditions. Catalysis takes place
                      at the heterobimetallic NiFe(CN)$_2$(CO) center, whose
                      multistep biosynthesis involves careful handling of two
                      transition metals as well as potentially harmful CO and
                      CN$^–$ molecules. Herein, we investigated the sequential
                      assembly of the [NiFe]-cofactor, previously based on
                      primarily indirect evidence, using four different purified
                      maturation intermediates of the catalytic subunit, HoxG, of
                      the O$_2$-tolerant membrane-bound hydrogenase from
                      Cupriavidus necator. These included the cofactor-free
                      apo-HoxG, a nickel-free version carrying only the
                      Fe(CN)$_2$(CO) fragment, a precursor that contained all
                      cofactor components but remained redox-inactive, and the
                      fully mature HoxG. Through biochemical analyses combined
                      with comprehensive spectroscopic investigation using
                      infrared, electronic paramagnetic resonance, Mössbauer,
                      X-ray absorption, and nuclear resonance vibrational
                      spectroscopies, we obtained detailed insight into the
                      sophisticated maturation process of [NiFe]-hydrogenase.},
      cin          = {DOOR ; HAS-User / FS-PET-S},
      cid          = {I:(DE-H253)HAS-User-20120731 /
                      I:(DE-H253)FS-PET-S-20190712},
      pnm          = {632 - Materials – Quantum, Complex and Functional
                      Materials (POF4-632) / 6G3 - PETRA III (DESY) (POF4-6G3) /
                      TIMB3 - Twin to Illuminate Metals in Biology and
                      Biocatalysis through Biospectroscopy (810856) /
                      G:(GEPRIS)390540038 - EXC 2008: Unifying Systems in
                      Catalysis "UniSysCat" (390540038) / FS-Proposal: I-20200452
                      (I-20200452)},
      pid          = {G:(DE-HGF)POF4-632 / G:(DE-HGF)POF4-6G3 /
                      G:(EU-Grant)810856 / G:(GEPRIS)390540038 /
                      G:(DE-H253)I-20200452},
      experiment   = {EXP:(DE-H253)P-P01-20150101},
      typ          = {PUB:(DE-HGF)25},
      doi          = {10.26434/chemrxiv-2022-jvtgw},
      url          = {https://bib-pubdb1.desy.de/record/481804},
}