Linked Life Data

7006765

Source:http://linkedlifedata.com/resource/pubmed/id/7006765

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1981-4-24
pubmed:abstractText
The periplasmic hydrogenase of Desulfovibrio desulfuricans was isolated and purified. Cells were washed with Tris-EDTA and the enzyme precipitated from the wash with ammonium sulfate. Absorption chromatography on DEAE and hydroxyapatite yielded the enzyme at better than 95% purity as judged by gel electrophoresis. The hydrogenase catalyzed the production of more than 9000 mumol H2/min mg protein(-1) from reduced methyl viologen at 37 degrees C. It is very stable and resists inactivation by heat (50% activity remained after 5 min in air at 65 degrees C) and by enzyme inhibitors (except N-ethylmaleimide and potassium ferricyanide). After storage in air at 4 degrees C for 1 month no activity was lost. The enzyme activity is sensitive to ionic environmental changes. With methyl viologen the optimum pH was 5.5 but with p-xylene polymeric viologen the optimum was about pH 7 but less sharp. The molecular weight was 47 X 10(3)(+/- 2 X 10(3), 52 X 10(3)(+/- X 10(3), and 56 X 19(3)(+/- 2 X 10(3) by SDS-gel electrophoresis, gel chromatography, and sedimentation equilibrium, respectively, and the isoelectric point was at pH 6.0. They enzyme might be useful in the production of hydrogen from water and solar energy.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0008-4166
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1214-23
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Purification and properties of the periplasmic hydrogenase from Desulfovibrio desulfuricans.
pubmed:publicationType
Journal Article