Heavy metal ions inhibit molybdoenzyme activity by binding to the dithiolene moiety of molybdopterin in Escherichia coli

@article{Neumann2008HeavyMI,
  title={Heavy metal ions inhibit molybdoenzyme activity by binding to the dithiolene moiety of molybdopterin in Escherichia coli},
  author={M. Neumann and S. Leimk{\"u}hler},
  journal={The FEBS Journal},
  year={2008},
  volume={275}
}
Molybdenum insertion into the dithiolene group on the 6‐alkyl side‐chain of molybdopterin is a highly specific process that is catalysed by the MoeA and MogA proteins in Escherichia coli. Ligation of molybdate to molybdopterin generates the molybdenum cofactor, which can be inserted directly into molybdoenzymes binding the molybdopterin form of the molybdenum cofactor, or is further modified in bacteria to form the dinucleotide form of the molybdenum cofactor. The ability of various metals to… Expand
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33 Citations
Background Citations
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Methods Citations
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Results Citations
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33 Citations

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Citation Type

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The biosynthesis of the molybdenum cofactors in Escherichia coli.
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The Biosynthesis of the Molybdenum Cofactor in Escherichia coli and Its Connection to FeS Cluster Assembly and the Thiolation of tRNA
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Protonation and Sulfido versus Oxo Ligation Changes at the Molybdenum Cofactor in Xanthine Dehydrogenase (XDH) Variants Studied by X-ray Absorption Spectroscopy.
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Identification of YdhV as the First Molybdoenzyme Binding a Bis-Mo-MPT Cofactor in Escherichia coli.
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Biosynthesis and Insertion of the Molybdenum Cofactor.
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Dithiolene complexes and the nature of molybdopterin
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The History of the Discovery of the Molybdenum Cofactor and Novel Aspects of its Biosynthesis in Bacteria.
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