@article{SchwanholdIobbiNivolLehmannetal.2018,
  author    = {Schwanhold, Nadine and Iobbi-Nivol, Chantal and Lehmann, Angelika and Leimk{\"u}hler, Silke},
  title     = {Same but different},
  series = {PLoS one},
  volume    = {13},
  journal   = {PLoS one},
  number    = {11},
  publisher = {PLoS},
  address   = {San Fransisco},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0201935},
  pages     = {24},
  year      = {2018},
  abstract  = {The maturation of bacterial molybdoenzymes is a complex process leading to the insertion of the bulky bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor into the apoenzyme. Most molybdoenzymes were shown to contain a specific chaperone for the insertion of the bis-MGD cofactor. Formate dehydrogenases (FDH) together with their molecular chaperone partner seem to display an exception to this specificity rule, since the chaperone FdhD has been proven to be involved in the maturation of all three FDH enzymes present in Escherichia colt. Multiple roles have been suggested for FdhD-like chaperones in the past, including the involvement in a sulfur transfer reaction from the L-cysteine desulfurase IscS to bis-MGD by the action of two cysteine residues present in a conserved CXXC motif of the chaperones. However, in this study we show by phylogenetic analyses that the CXXC motif is not conserved among FdhD-like chaperones. We compared in detail the FdhD-like homologues from Rhodobacter capsulatus and E. colt and show that their roles in the maturation of FDH enzymes from different subgroups can be exchanged. We reveal that bis-MGDbinding is a common characteristic of FdhD-like proteins and that the cofactor is bound with a sulfido-ligand at the molybdenum atom to the chaperone. Generally, we reveal that the cysteine residues in the motif CXXC of the chaperone are not essential for the production of active FDH enzymes.},
  language  = {en}
}
@misc{HartmannSchwanholdLeimkuehler2015,
  author    = {Hartmann, Tobias and Schwanhold, Nadine and Leimk{\"u}hler, Silke},
  title     = {Assembly and catalysis of molybdenum or tungsten-containing formate dehydrogenases from bacteria},
  series = {Biochimica et biophysica acta : Proteins and proteomics},
  volume    = {1854},
  journal   = {Biochimica et biophysica acta : Proteins and proteomics},
  number    = {9},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1570-9639},
  doi       = {10.1016/j.bbapap.2014.12.006},
  pages     = {1090 -- 1100},
  year      = {2015},
  abstract  = {The global carbon cycle depends on the biological transformations of C-1 compounds, which include the reductive incorporation of CO2 into organic molecules (e.g. in photosynthesis and other autotrophic pathways), in addition to the production of CO2 from formate, a reaction that is catalyzed by formate dehydrogenases (FDHs). FDHs catalyze, in general, the oxidation of formate to CO2 and H+. However, selected enzymes were identified to act as CO2 reductases, which are able to reduce CO2 to formate under physiological conditions. This reaction is of interest for the generation of formate as a convenient storage form of H-2 for future applications. Cofactor-containing FDHs are found in anaerobic bacteria and archaea, in addition to facultative anaerobic or aerobic bacteria. These enzymes are highly diverse and employ different cofactors such as the molybdenum cofactor (Moco), FeS clusters and flavins, or cytochromes. Some enzymes include tungsten (W) in place of molybdenum (Mo) at the active site. For catalytic activity, a selenocysteine (SeCys) or cysteine (Cys) ligand at the Mo atom in the active site is essential for the reaction. This review will focus on the characterization of Mo- and W-containing FDHs from bacteria, their active site structure, subunit compositions and its proposed catalytic mechanism. We will give an overview on the different mechanisms of substrate conversion available so far, in addition to providing an outlook on bio-applications of FDHs. This article is part of a Special Issue entitled: Cofactor-dependent proteins: evolution, chemical diversity and bio-applications. (C) 2014 Elsevier B.V. All rights reserved.},
  language  = {en}
}
@phdthesis{Schwanhold2018,
  author    = {Schwanhold, Nadine},
  title     = {Die Funktion und Spezifit{\"a}t der Molybd{\"a}n-Cofaktor-bindenden Chaperone f{\"u}r die Formiat-Dehydrogenasen aus Escherichia coli und Rhodobacter capsulatus},
  school      = {Universit{\"a}t Potsdam},
  pages     = {132},
  year      = {2018},
  language  = {de}
}