Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Orii, Y.
Right arrow Articles by Webster, D. A.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Orii, Y.
Right arrow Articles by Webster, D. A.
Agricola
Right arrow Articles by Orii, Y.
Right arrow Articles by Webster, D. A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 1977, Vol. 18, No. 3 521-526
© 1977

Article

Oxygenated cytochrome o (Vitreoscilla) formed by treating oxidized cytochrome with superoxide anion

Yutaka Orii1 and Dale A. Webster2

1 Department of Biology, Faculty of Science, Osaka University Toyonaka, Osaka 560, Japan
2 Department of Biology, Illinois Institute of Technology Chicago, Illinois 60616, U.S.A.

Oxygenated cytochrome o can be formed experimentally in two ways, i) by reaction of reduced cytochrome o with molecular oxygen, or ii) by reaction of oxidized cytochrome o with superoxide anion generated by the action of the xanthine oxidase system. It is thermodynamically feasible for oxidized cytochrome o plus O2–, and reduced cytochrome o plus O2 to appear as intermediates in reactions i) and ii), respectively.

Superoxide dismutase completely inhibits the xanthine oxidase-catalyzed conversion of oxidized cytochrome o into the oxygenated form but it has relatively little effect on the oxygenated cytochrome o formation in the reaction system consisting of NADH, NADH-cytochrome o reductase, and cytochrome o. Thus, if superoxide anion does play a significant role in the latter system it must be efficiently coupled to react with cytochrome o and inaccessible to superoxide dismutase. Direct electron transfer from the reductase to the cytochrome without the involvement of superoxide anion is an alternative mechanism.

(Received December 16, 1976; )
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
K.-W. Park, K.-J. Kim, A. J. Howard, B. C. Stark, and D. A. Webster
Vitreoscilla Hemoglobin Binds to Subunit I of Cytochrome bo Ubiquinol Oxidases
J. Biol. Chem., August 30, 2002; 277(36): 33334 - 33337.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.