1998/12/01 by Caroline Kisker, Hermann Schindelin, Dietmar Baas +3 · 2 citations
Energy · Chemistry · #Metalloenzymes and iron-sulfur proteins #Electrocatalysts for Energy Conversion #Metal-Catalyzed Oxygenation Mechanisms
paper · doi:10.1111/j.1574-6976.1998.tb00384.x
openalex publication_date 1998/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/29
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.