@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}
}
@article{BoehmerHartmannLeimkuehler2014,
  author    = {Boehmer, Nadine and Hartmann, Tobias and Leimk{\"u}hler, Silke},
  title     = {The chaperone FdsC for Rhodobacter capsulatus formate dehydrogenase binds the bis-molybdopterin guanine dinucleotide cofactor},
  series = {FEBS letters : the journal for rapid publication of short reports in molecular biosciences},
  volume    = {588},
  journal   = {FEBS letters : the journal for rapid publication of short reports in molecular biosciences},
  number    = {4},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0014-5793},
  doi       = {10.1016/j.febslet.2013.12.033},
  pages     = {531 -- 537},
  year      = {2014},
  abstract  = {Molybdoenzymes are complex enzymes in which the molybdenum cofactor (Moco) is deeply buried in the enzyme. Most molybdoenzymes contain a specific chaperone for the insertion of Moco. For the formate dehydrogenase FdsGBA from Rhodobacter capsulatus the two chaperones FdsC and FdsD were identified to be essential for enzyme activity, but are not a subunit of the mature enzyme. Here, we purified and characterized the FdsC protein after heterologous expression in Escherichia coli. We were able to copurify FdsC with the bound Moco derivate bis-molybdopterin guanine dinucleotide. This cofactor successfully was used as a source to reconstitute the activity of molybdoenzymes. Structured summary of protein interactions: FdsC and FdsC bind by molecular sieving (View interaction) FdsD binds to RcMobA by surface plasmon resonance (View interaction) FdsC binds to RcMobA by surface plasmon resonance (View interaction) FdsC binds to FdsA by surface plasmon resonance (View interaction)},
  language  = {en}
}