Open AccessCrystallization and preliminary X‐ray analysis of the tungsten‐dependent acetylene hydratase from Pelobacter acetylenicus
Author(s) -
Einsle Oliver,
Niessen Holger,
Abt Dietmar J.,
Seiffert Grazyna,
Schink Bernhard,
Huber Robert,
Messerschmidt Albrecht,
Kroneck Peter M. H.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910500374x
Subject(s) - disproportionation , acetylene , crystallization , tungsten , chemistry , acetaldehyde , nuclear chemistry , ethanol , organic chemistry , catalysis
Acetylene hydratase is a tungsten‐containing hydroxylase that converts acetylene to acetaldehyde in a unique reaction that requires a strong reductant. The subsequent disproportionation of acetaldehyde yields acetate and ethanol. Crystals of the tungsten/iron–sulfur protein acetylene hydratase from Pelobacter acetylenicus strain WoAcy 1 (DSM 3246) were grown by the vapour‐diffusion method in an N 2 /H 2 atmosphere using polyethylene glycol as precipitant. Growth of crystals suitable for X‐ray analysis strictly depended on the presence of Ti III citrate or dithionite as reducing agents.