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Insights into Reductive Dehalogenase Function Obtained from Crystal Structures

  • Holger Dobbek
  • David LeysEmail author
Chapter

Abstract

Reductive dehalogenases are a class of corrinoid and [4Fe–4S] cluster-dependent enzymes that are arguably key to organohalide respiration. Recently, the first crystal structures for these enzymes were reported, including one representative of both a respiratory as well as a nonrespiratory catabolic reductive dehalogenase. The comparison made between both structures establishes two highly conserved elements: the configuration of the redox chain within the protein and the Tyr–Lys/Arg active site dyad involved in proton transfer to the substrate. In contrast, the substrate binding elements are highly distinct. These insights serve to guide further study of RdhA structure–function relationships.

Keywords

Direct Electron Transfer Halogen Bond Sulfur Cluster Substrate Binding Pocket Reductive Dehalogenases 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 2016

Authors and Affiliations

  1. 1.Institut für Biologie, Strukturbiologie/BiochemieHumboldt-Universität zu BerlinBerlinGermany
  2. 2.MIB, University of ManchesterManchesterUK

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