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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