@misc{LeimkuehlerWuebbensRajagopalan2011,
  author    = {Leimk{\"u}hler, Silke and Wuebbens, Margot M. and Rajagopalan, K. V.},
  title     = {The history of the discovery of the molybdenum cofactor and novel aspects of its biosynthesis in bacteria},
  series = {Coordination chemistry reviews},
  volume    = {255},
  journal   = {Coordination chemistry reviews},
  number    = {9-10},
  publisher = {Elsevier},
  address   = {Lausanne},
  issn      = {0010-8545},
  doi       = {10.1016/j.ccr.2010.12.003},
  pages     = {1129 -- 1144},
  year      = {2011},
  abstract  = {The biosynthesis of the molybdenum cofactor in bacteria is described with a detailed analysis of each individual reaction leading to the formation of stable intermediates during the synthesis of molybdopterin from GTP. As a starting point, the discovery of molybdopterin and the elucidation of its structure through the study of stable degradation products are described. Subsequent to molybdopterin synthesis, the molybdenum atom is added to the molybdopterin dithiolene group to form the molybdenum cofactor. This cofactor is either inserted directly into specific molybdoenzymes or is further modified by the addition of nucleotides to molybdopterin phosphate group or the replacement of ligands at the molybdenum center.},
  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}
}