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Is the Paracoccus halodenitrificans ATPase a chimeric enzyme?Membranes from Paracoccus halodenitrificans contain an ATPase that is most active in the absence of NaCl. The most unusual characteristic of the enzyme is its pattern of sensitivity to various inhibitors. Azide and rhodamine 6G, inhibitors of F1F0-ATPases, inhibit ATP hydrolysis as do bafilomycin A1, concanamycin A (folimycin), N-ethylmaleimide, and p-chloromercuriphenylsulfonate which are inhibitors of vacuolar ATPases. This indiscriminate sensitivity suggests that this ATPase may be a hybrid and that caution should be exercised when using inhibition as a diagnostic for distinguishing between F1F0-ATPases and vacuolar ATPases.
Document ID
20040112211
Acquisition Source
Ames Research Center
Document Type
Reprint (Version printed in journal)
Authors
Hochstein, L. I.
(NASA Ames Research Center Moffett Field CA United States)
Date Acquired
August 21, 2013
Publication Date
June 15, 1996
Publication Information
Publication: FEMS microbiology letters
Volume: 140
Issue: 1
ISSN: 0378-1097
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other
Keywords
NASA Center ARC
NASA Discipline Exobiology

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