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Electron transport in Paracoccus halodenitrificans and the role of UbiquinoneThe membrane-bound NADH oxidase of Paracoccus halodenitrificans was inhibited by dicoumarol, 2-n-heptyl-4-hydroxyquinoline-N-oxide (HQNO), and exposure to ultraviolet light (at 366 nm). When the membranes were extracted with n-pentane, NADH oxidase activity was lost. Partial restoration was achieved by adding the ubiquinone fraction extracted from the membranes. Succinate oxidation was not inhibited by dicoumarol or HQNO but was affected by ultraviolet irradiation or n-pentane extraction. However, the addition of the ubiquinone fraction to the n-pentane-extracted membranes did not restore enzyme activity. These observations suggested the reducing equivalents from succinate entered the respiratory chain on the oxygen side of the HQNO-sensitive site and probably did not proceed through a quinone.
Document ID
19840063763
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Hochstein, L. I.
(NASA Ames Research Center Moffett Field, CA, United States)
Cronin, S. E.
(NASA Ames Research Center Extraterrestrial Research Div., Moffett Field, CA, United States)
Date Acquired
August 12, 2013
Publication Date
January 1, 1984
Publication Information
Publication: Canadian Journal of Microbiology
Volume: 30
Issue: 5, 19
ISSN: 0008-4166
Subject Category
Life Sciences (General)
Accession Number
84A46550
Distribution Limits
Public
Copyright
Other

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