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Mitochondrial nucleoside diphosphate kinase: Mode of interaction with the outer mitochondrial membrane and proportion of catalytic activity functionally coupled to oxidative phosphorylation

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Abstract

In the present study, we found that ionic interactions are not essential for the binding of nucleoside diphosphate kinase of liver mitochondria outer compartment to outer mitochondrial membrane and that the proportion of the enzyme activity involved in functional coupling with oxidative phosphorylation (we demonstrated the existence of functional coupling earlier) is only 17%. Additional evidence was obtained that functionally coupled activity of nucleoside diphosphate kinase is associated with the outer surface of mitochondria. Dextran (10%) did not increase functional coupling. The physological importance of these effects is discussed.

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Abbreviations

AP5A:

p1p5-di(adenosine-5′)pentaphosphate

CPK:

muscle creatine phosphokinase

FCCP:

carbonyl cyanide p-(trifluoromethoxy)phenylhydrazone

HK:

hexokinase

mAK:

mitochondrial adenylate kinase

NDPK:

nucleoside diphosphate kinase

omNDPK:

outer mitochondrial membrane bound NDPK

RCR:

respiratory control ratio

yHK:

yeast HK

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Authors and Affiliations

  1. Department of Biochemistry, Faculty of Biology, Lomonosov Moscow State University, 119991, Moscow, Russia

    T. Yu. Lipskaya & V. V. Voinova

Authors
  1. T. Yu. Lipskaya
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  2. V. V. Voinova
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Correspondence to T. Yu. Lipskaya.

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Published in Russian in Biokhimiya, 2008, Vol. 73, No. 3, pp. 395–407.

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Lipskaya, T.Y., Voinova, V.V. Mitochondrial nucleoside diphosphate kinase: Mode of interaction with the outer mitochondrial membrane and proportion of catalytic activity functionally coupled to oxidative phosphorylation. Biochemistry Moscow 73, 321–331 (2008). https://doi.org/10.1134/S0006297908030139

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  • DOI: https://doi.org/10.1134/S0006297908030139

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