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Nitric oxide is a potent inhibitor of the cbb(3)-type heme-copper oxidases
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 3
2015 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 589, no 11, 1214-1218 p.Article in journal (Refereed) Published
Abstract [en]

C-type heme-copper oxidases terminate the respiratory chain in many pathogenic bacteria, and will encounter elevated concentrations of NO produced by the immune defense of the host. Thus, a decreased sensitivity to NO in C-type oxidases would increase the survival of these pathogens. Here we have compared the inhibitory effect of NO in C-type oxidases to that in the mitochondrial A-type. We show that O-2-reduction in both the Rhodobacter sphaeroides and Vibrio cholerae C-type oxidases is strongly and reversibly inhibited by submicromolar NO, with an inhibition pattern similar to the A-type. Thus, NO tolerance in pathogens with a C-type terminal oxidase has to rely mainly on other mechanisms.

Place, publisher, year, edition, pages
2015. Vol. 589, no 11, 1214-1218 p.
Keyword [en]
Respiration, Catalytic site, Cytochrome c oxidase, IC50, Nitrite
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-117776DOI: 10.1016/j.febslet.2015.03.033ISI: 000353833900007OAI: oai:DiVA.org:su-117776DiVA: diva2:817604
Available from: 2015-06-05 Created: 2015-06-01 Last updated: 2017-12-04Bibliographically approved

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