@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}
}
@misc{IobbiNivolLeimkuehler2013,
  author    = {Iobbi-Nivol, Chantal and Leimk{\"u}hler, Silke},
  title     = {Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli},
  series = {Biochimica et biophysica acta : Bioenergetics},
  volume    = {1827},
  journal   = {Biochimica et biophysica acta : Bioenergetics},
  number    = {8-9},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0005-2728},
  doi       = {10.1016/j.bbabio.2012.11.007},
  pages     = {1086 -- 1101},
  year      = {2013},
  abstract  = {Molybdenum cofactor (Moco) biosynthesis is an ancient, ubiquitous, and highly conserved pathway leading to the biochemical activation of molybdenum. Moco is the essential component of a group of redox enzymes, which are diverse in terms of their phylogenetic distribution and their architectures, both at the overall level and in their catalytic geometry. A wide variety of transformations are catalyzed by these enzymes at carbon, sulfur and nitrogen atoms, which include the transfer of an oxo group or two electrons to or from the substrate. More than 50 molybdoenzymes were identified in bacteria to date. In molybdoenzymes Mo is coordinated to a dithiolene group on the 6-alkyl side chain of a pterin called molybdopterin (MPT). The biosynthesis of Moco can be divided into four general steps in bacteria: I) formation of the cyclic pyranopterin monophosphate, 2) formation of MPT, 3) insertion of molybdenum into molybdopterin to form Moco, and 4) additional modification of Moco with the attachment of GMP or CMP to the phosphate group of MPT, forming the dinucleotide variant of Moco. This review will focus on molybdoenzymes, the biosynthesis of Moco, and its incorporation into specific target proteins focusing on Escherichia coli. This article is part of a Special Issue entitled: Metals in Bioenergetics and Biomimetics Systems.},
  language  = {en}
}