These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: The K(+)-ionophores nonactin and valinomycin interact differently with the protein of reconstituted cytochrome c oxidase.
    Author: Steverding D, Kadenbach B.
    Journal: J Bioenerg Biomembr; 1990 Apr; 22(2):197-205. PubMed ID: 2158497.
    Abstract:
    The K(+)-ionophores valinomycin and nonactin induce a qualitatively identical change of the visible spectrum of isolated oxidized cytochrome c oxidase (red shift), but the amplitude is half with nonactin. Valinomycin, in the presence or absence of a protonophore, stimulates the respiration of the reconstituted enzyme to a higher extent than nonactin and results in a higher Km for cytochrome c. In contrast, nonactin causes a fivefold rate of proton conductivity across a liposomal membrane, after induction of a K(+)-diffusion potential. The data indicate that respiratory control by these antibiotics is not only due to degradation of a membrane potential, but rather to specific interaction with and modification of cytochrome c oxidase.
    [Abstract] [Full Text] [Related] [New Search]