Open AccessPurification, crystallization and preliminary crystallographic analysis of the [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough
Author(s) -
Marques Marta,
Coelho Ricardo,
Pereira Inês A. C.,
Matias Pedro M.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109031261
Subject(s) - selenocysteine , desulfovibrio vulgaris , hydrogenase , monoclinic crystal system , crystallization , crystallography , chemistry , x ray crystallography , catalysis , materials science , crystal structure , enzyme , biochemistry , diffraction , bacteria , biology , organic chemistry , physics , cysteine , optics , genetics
The [NiFeSe] hydrogenases belong to a subgroup of the [NiFe] proteins in which a selenocysteine is a ligand of the Ni. These enzymes demonstrate interesting catalytic properties, showing a very high H 2 ‐producing activity that is sustained in the presence of low O 2 concentrations. The purification, crystallization and preliminary X‐ray diffraction analysis of the [NiFeSe] hydrogenase isolated from Desulfovibrio vulgaris Hildenborough are reported. Crystals of the soluble form of this hydrogenase were obtained using 20% PEG 1500 as a precipitant and belonged to the monoclinic space group P 2 1 , with unit‐cell parameters a = 60.57, b = 91.05, c = 66.85 Å, β = 101.46°. Using an in‐house X‐ray diffraction system, they were observed to diffract X‐rays to 2.4 Å resolution.