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Dimer-dimer interactions in octameric mitochondrial creatine kinase

M Gross1, T Wallimann

  • 1Swiss Federal Institute of Technology, Institute for Cell Biology, ETH-Hönggerberg, Zürich.

Biochemistry
|May 23, 1995
PubMed
Summary
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Mitochondrial creatine kinase (Mi-CK) octamer stability is influenced by temperature, pH, and substrates. Hydrophobic interactions stabilize Mi-CK octamers, suggesting slow regulatory roles in energy metabolism.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Mitochondrial creatine kinase (Mi-CK) exists as interconvertible octamers and dimers.
  • Understanding Mi-CK oligomerization is crucial for elucidating its role in cellular energy metabolism.

Purpose of the Study:

  • Investigate the kinetic and thermodynamic stability of wild-type and mutant chicken sarcomeric Mi-CK octamers.
  • Identify factors regulating the in vivo octamer/dimer ratio and the nature of octamer-stabilizing interactions.

Main Methods:

  • Kinetic and thermodynamic analysis of wild-type and mutant Mi-CK.
  • Experiments conducted at varying temperatures, pH, salt, and substrate concentrations.
  • Utilized transition state analogue complex (TSAC) to probe octamer decay.

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Main Results:

  • Octamer decay accelerated with increasing temperature (up to 28°C) and pH for wild-type Mi-CK.
  • Substrate binding and TSAC induced octamer-destabilizing conformations.
  • Hydrophobic and polar interactions stabilize octamers; hydrophobic interactions dominate.
  • Mutant W264C showed altered temperature dependence, suggesting abolished hydrophobic interactions.

Conclusions:

  • Mi-CK octamer-dimer transitions are likely involved in slow, long-term modulations of mitochondrial energy metabolism, not rapid regulation.
  • Hydrophobic interactions play a significant role in maintaining Mi-CK octamer stability.