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An Overview of Ubiquinone Proteins

  • Tsoo E. King

Summary

Ubiquinone (coenzyme Q) may serve as a respiratory carrier only when it is bound to a protein. Q may be considered as a prosthetic group, i. e. coenzyme, which can freely dissociate and associate with protein. So far three classes of Q-proteins have been found. QP-S is the immediate electron acceptor of succinate dehydrogenase (SDH). The reconstitution of succinate-ubiquinone reductase needs only SDH and QP-S independent of any cytochrome. QP-S has been isolated to pure form but its high hydrophobic nature prevents the complete determination by chemical means of primary structure.

QP-C acts in the cytochromes b and c1 region, has been purified and amino acid sequence determined. We do not know whether there is second QP-C to fulfil Qo and Qi theory. QP-N exists in the NADH-ubiquinone reductase segment which is free from SDH and cytochrome oxidase and nearly free (<0.06 nmol per mg protein) of cytochromes b and c1. The protein moiety of Q-protein not only stabilizes the ubisemiquinone but also dictates the site or sites where the QP acts on the respiratory chain.

Keywords

Respiratory Chain Microwave Power Succinate Dehydrogenase Cytochrome B560 Sodium Dodecyl Sulfate Solution 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Tsoo E. King
    • 1
    • 2
  1. 1.Institute of Structural & Functional StudiesUniversity City Science CenterPhiladelphiaUSA
  2. 2.Department of Biochemistry & BiophysicsUniversity of PennsylvaniaPhiladelphiaUSA

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