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

129 Scopus citations

Abstract

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
Volume22
Issue number5
DOIs
StatePublished - 1998
Externally publishedYes

Keywords

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

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