@misc{MendelLeimkuehler2015,
  author    = {Mendel, Ralf R. and Leimk{\"u}hler, Silke},
  title     = {The biosynthesis of the molybdenum cofactors},
  series = {Journal of biological inorganic chemistry},
  volume    = {20},
  journal   = {Journal of biological inorganic chemistry},
  number    = {2},
  publisher = {Springer},
  address   = {New York},
  issn      = {0949-8257},
  doi       = {10.1007/s00775-014-1173-y},
  pages     = {337 -- 347},
  year      = {2015},
  abstract  = {The biosynthesis of the molybdenum cofactors (Moco) 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 to date. In all molybdoenzymes except nitrogenase, molybdenum 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 three general steps, with a fourth one present only in bacteria and archaea: (1) 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 in bacteria with the attachment of a nucleotide to the phosphate group of MPT, forming the dinucleotide variant of Moco. This review will focus on the biosynthesis of Moco in bacteria, humans and plants.},
  language  = {en}
}
@article{FrascaMilanGuietetal.2013,
  author    = {Frasca, Stefano and Milan, Anabel Molero and Guiet, Amandine and Goebel, Caren and Perez-Caballero, Fernando and Stiba, Konstanze and Leimk{\"u}hler, Silke and Fischer, Anna and Wollenberger, Ursula},
  title     = {Bioelectrocatalysis at mesoporous antimony doped tin oxide electrodes-Electrochemical characterization and direct enzyme communication},
  series = {ELECTROCHIMICA ACTA},
  volume    = {110},
  journal   = {ELECTROCHIMICA ACTA},
  number    = {2},
  publisher = {PERGAMON-ELSEVIER SCIENCE LTD},
  address   = {OXFORD},
  issn      = {0013-4686},
  doi       = {10.1016/j.electacta.2013.03.144},
  pages     = {172 -- 180},
  year      = {2013},
  abstract  = {In this paper we report immobilization and bioelectrocatalysis of human sulfite oxidase (hSO) on nanostructured antimony doped tin oxide (ATO) thin film electrodes. Two types of ATO thin film electrodes were prepared via evaporation induced self-assembly of ATO nanoparticle sols. The use of a porogen results in different porosity and film thickness. Nevertheless both electrode types reveal similar quasi reversible electrochemical behavior for positive and negatively charged small mediators. Facile and durable immobilization of catalytically active enzyme in a direct electron transfer configuration was achieved without further chemical modification of the ATO surfaces. Interestingly, the binding of hSO onto the ATO surface seems to be not only of electrostatic nature, but also originates from a strong interaction between the histidine-tag of the enzyme and the supporting material. This is suggested from stable sulfite dependent bioelectrocatalytic signals at high ionic strength and imidazole desorption experiments. As such, ATO appears as a promising conductive platform for the immobilization of complex enzymes and their application in bioelectrocatalysis. (C) 2013 Elsevier Ltd. All rights reserved.},
  language  = {en}
}