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: Molecular characterization of two spontaneous antimycin A resistant mutants of Rhodospirillum rubrum.
    Author: Uhrig JF, Jakobs CU, Majewski C, Trebst A.
    Journal: Biochim Biophys Acta; 1994 Sep 27; 1187(3):347-53. PubMed ID: 7918532.
    Abstract:
    Antimycin A is an inhibitor of cytochrome bc1 complexes acting at the quinone reducing site (Qi) of the cytochrome b subunit. We report here the isolation and molecular characterization of two spontaneous mutants of the purple non-sulfur bacterium Rhodospirillum rubrum resistant to this inhibitor. In the two mutants antimycin A resistance was found to be conferred by replacement of an aspartate residue at position 243 of the cytochrome b polypeptide chain, in one case by histidine and in the other by glutamate. The mutants exhibit cross-resistance to aurachin C but not to aurachin D. The exchange of Asp-243 does not only diminish the antimycin sensitivity of the isolated cytochrome bc1 complexes but also has effects on the function of the quinone reducing site (Qi). Oxidant-induced reduction of cytochrome b, requiring addition of antimycin A in the wild type, is already at a maximum in the absence of antimycin A. This indicates a diminished electron flow between heme b-566 and ubiquinone at the quinone reducing site (Qi) of cytochrome b.
    [Abstract] [Full Text] [Related] [New Search]