@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}
}
@article{DahlRadonBuehningetal.2013,
  author    = {Dahl, Jan-Ulrik and Radon, Christin and B{\"u}hning, Martin and Nimtz, Manfred and Leichert, Lars I. and Denis, Yann and Jourlin-Castelli, Cecile and Iobbi-Nivol, Chantal and Mejean, Vincent and Leimk{\"u}hler, Silke},
  title     = {The Sulfur Carrier Protein TusA Has a Pleiotropic Role in Escherichia coli That Also Affects Molybdenum Cofactor Biosynthesis},
  series = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  volume    = {288},
  journal   = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  number    = {8},
  publisher = {AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC},
  address   = {BETHESDA},
  issn      = {0021-9258},
  doi       = {10.1074/jbc.M112.431569},
  pages     = {5426 -- 5442},
  year      = {2013},
  abstract  = {The Escherichia coli L-cysteine desulfurase IscS mobilizes sulfur from L-cysteine for the synthesis of several biomolecules such as iron-sulfur (FeS) clusters, molybdopterin, thiamin, lipoic acid, biotin, and the thiolation of tRNAs. The sulfur transfer from IscS to various biomolecules is mediated by different interaction partners (e.g. TusA for thiomodification of tRNAs, IscU for FeS cluster biogenesis, and ThiI for thiamine biosynthesis/tRNA thiolation), which bind at different sites of IscS. Transcriptomic and proteomic studies of a Delta tusA strain showed that the expression of genes of the moaABCDE operon coding for proteins involved in molybdenum cofactor biosynthesis is increased under aerobic and anaerobic conditions. Additionally, under anaerobic conditions the expression of genes encoding hydrogenase 3 and several molybdoenzymes such as nitrate reductase were also increased. On the contrary, the activity of all molydoenzymes analyzed was significantly reduced in the Delta tusA mutant. Characterization of the Delta tusA strain under aerobic conditions showed an overall low molybdopterin content and an accumulation of cyclic pyranopterin monophosphate. Under anaerobic conditions the activity of nitrate reductase was reduced by only 50\%, showing that TusA is not essential for molybdenum cofactor biosynthesis. We present a model in which we propose that the direction of sulfur transfer for each sulfur-containing biomolecule is regulated by the availability of the interaction partner of IscS. We propose that in the absence of TusA, more IscS is available for FeS cluster biosynthesis and that the overproduction of FeS clusters leads to a modified expression of several genes.},
  language  = {en}
}