A structural comparison of molybdenum cofactor-containing enzymes

Caroline Kisker, Hermann Schindelin, Dietmar Baas, Janos Rétey, Rainer U. Meckenstock, Peter M.H. Kroneck

Research output: Contribution to journalArticlepeer-review

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This work gives an overview of the recent achievements which have contributed to the understanding of the structure and function of molybdenum and tungsten enzymes. Known structures of molybdo-pterin cofactor-containing enzymes will be described briefly and the structural differences between representatives of the same and different families will be analyzed. This comparison will show that the molybdo-pterin cofactor-containing enzymes represent a very heterogeneous group with differences in overall enzyme structure, cofactor composition and stoichiometry, as well as differences in the immediate molybdenum environment. Two recently discovered molybdo-pterin cofactor-containing enzymes will be described with regard to molecular and EPR spectroscopic properties, pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici and acetylene hydratase from Pelobacter acetylenicus. On the basis of its amino acid sequence, transhydroxylase can be classified as a member of the dimethylsulfoxide reductase family, whereas classification of the tungsten/molybdenum-containing acetylene hydratase has to await the determination of its amino acid sequence. Copyright (C) 1999 Federation of European Microbiological Societies.

Original languageEnglish
Pages (from-to)503-521
Number of pages19
JournalFEMS Microbiology Reviews
Issue number5
StatePublished - 1998
Externally publishedYes


  • Acetylene hydratase
  • Iron-sulfur cluster
  • Molybdenum enzymes
  • Molybdo-pterin
  • Transhydroxylase
  • Tungsten enzymes


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