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Vanadate inhibition of mitochondrial respiration and H+ ATPase activity in Saccharomyces cerevisiae

Henderson, G.E., Evans, I.H., Bruce, Ian J. (1989) Vanadate inhibition of mitochondrial respiration and H+ ATPase activity in Saccharomyces cerevisiae. Yeast, 5 (1). pp. 73-77. ISSN 0749-503X. (doi:10.1002/yea.320050109) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:71991)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1002/yea.320050109

Abstract

The effects of vandate on mitochondrial respiration and H+ ATPase activity in Saccharomyces cerevisiae were studied. A 50 inhibition of oxygen uptake in isolated mitochondria was produced by 4·4 mM?V2O5. Activity of H+ ATPase in whole mitochondria was inhibited by 50 by 5·5 ?M?V2O5, in submitochondrial particles by 55 ?M?V2O5; and in the chloroform?released H+ ATPase by 0·5 mM?V2O5. Vandate was also found to relieve growth inhibition caused by the mitochondrial H+ ATPase inhibitors NN??decyclohexylcarbodiimide and oligomycin. These results imply that vanadate could affect mitochondrial respiration by interacting with the H+ ATPase in S. cerevisiae.

Item Type: Article
DOI/Identification number: 10.1002/yea.320050109
Uncontrolled keywords: adenosine triphosphatase; Proton Translocating ATPases; proton transporting adenosine triphosphatase; vanadic acid, article; drug effect; enzymology; metabolism; mitochondrion; oxygen consumption; Saccharomyces cerevisiae, Adenosinetriphosphatase; Mitochondria; Oxygen Consumption; Proton-Translocating ATPases; Saccharomyces cerevisiae; Vanadates
Divisions: Faculties > Sciences > School of Physical Sciences
Faculties > Sciences > School of Physical Sciences > Functional Materials Group
Depositing User: Ian Bruce
Date Deposited: 30 Jan 2019 17:27 UTC
Last Modified: 30 May 2019 08:50 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/71991 (The current URI for this page, for reference purposes)
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