Crystallization and preliminary X-ray analysis of the tungsten-dependent acetylene hydratase from Pelobacter acetylenicus.

Structural aspects of molybdenum-transhydroxylase from Pelobacter acidigallici and tungsten-acetylene hydratase from Pelobacter acetylenicus

Tungsten-acetylene hydratase from Pelobacter acetylenicus and molybdenum-transhydroxylase from Pelobacter acidigallici: Two novel molybdopterin and iron-sulfur containing enzymes

Acetylene Hydratase from Pelobacter acetylenicus : functional Studies on a Gas-Processing Tungsten, Iron-Sulfur Enzyme by Site Directed Mutagenesis and Crystallography

Purification and characterization of acetylene hydratase of Pelobacter acetylenicus, a tungsten iron-sulfur protein.

Acetylene hydratase of the mesophilic fermenting bacterium Pelobacter acetylenicus catalyzes the hydration of acetylene to acetaldehyde. Growth of P. acetylenicus with acetylene and specific acetylene hydratase activity depended on tungstate or, to a lower degree, molybdate supply in the medium. The specific enzyme activity in cell extract was highest after growth in the presence of tungstate. ...

A structural comparison of molybdenum cofactor-containing enzymes.

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 ...