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Purification and properties of a dissimilatory nitrate reductase from Haloferax denitrificansA membrane-bound nitrate reductase (nitrite:(acceptor) oxidoreductase, EC 1.7.99.4) from the extremely halophilic bacterium Haloferax denitrificans was solubilized by incubating membranes in buffer lacking NaCl and purified by DEAE, hydroxylapatite, and Sepharose 6B gel filtration chromatography. The purified nitrate reductase reduced chlorate and was inhibited by azide and cyanide. Preincubating the enzyme with cyanide increased the extent of inhibition which in turn was intensified when dithionite was present. Although cyanide was a noncompetitive inhibitor with respect to nitrate, nitrate protected against inhibition. The enzyme, as isolated, was composed of two subunits (Mr 116,000 and 60,000) and behaved as a dimer during gel filtration (Mr 380,000). Unlike other halobacterial enzymes, this nitrate reductase was most active, as well as stable, in the absence of salt.
Document ID
20050000845
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Hochstein, L. I.
(NASA Ames Research Center Moffett Field, CA United States)
Lang, F.
Date Acquired
August 22, 2013
Publication Date
August 1, 1991
Publication Information
Publication: Archives of biochemistry and biophysics
Volume: 288
Issue: 2
ISSN: 0003-9861
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other

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