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

Search MEDLINE/PubMed


  • Title: [The structural membrane control of the reduction of exogenous quinones catalysed by mitochondrial 2-methyl-1,4-naphthoquinone reductase].
    Author: Konev SV, Sukhodolets IG, Volotovskiĭ ID, Titovets EP.
    Journal: Mol Biol (Mosk); 1982; 16(6):1279-83. PubMed ID: 7155143.
    Abstract:
    The catalytic parameters of mitochondrial 2-methyl-1, 4-naphthoquinone-reductase were studied. Maximal velocity and Michaelis constant of quinone-reducing reaction were shown to depend strongly on the functional state of mitochondria (I, II and IV Chance's states). The changes in catalytic parameters were found for four quinone substrates essentially varying in their structures. For the same conditions the Michaelis constant of isolated enzyme remains unchanged. The data obtained indicate the possibility to control the activity and substrate specificity by structural rearrangements within the biological membrane.
    [Abstract] [Full Text] [Related] [New Search]