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Functional equivalence of monomeric (shark) and dimeric (bovine) cytochrome c oxidase.

Publication ,  Journal Article
Bickar, D; Lehninger, A; Brunori, M; Bonaventura, J; Bonaventura, C
Published in: Journal of inorganic biochemistry
March 1985

Cytochrome c oxidase isolated from hammerhead shark red muscle is monomeric in relation to the dimeric form of isolated bovine cytochrome c oxidase but in other ways bears a close resemblance to the enzyme isolated from mammalian tissue [1, 2]. Comparative studies of shark and bovine cytochrome c oxidase were extended to address the degree of functional similarity between the monomeric (shark) and dimeric (bovine) enzymes in the kinetics of peroxide binding and in the extent to which the catalytic action of the enzymes in vesicles can establish a proton gradient. Although the kinetics of peroxide binding and the proton pumping processes are complex, the dimeric and monomeric forms are quite similar with respect to these functional attributes. The kinetic heterogeneity of the process of peroxide binding is expressed in the shark enzyme as well as in the bovine enzyme, and both types of enzymes in vesicles can generate transmembrane proton gradients. On this basis we conclude that the dimeric state of isolated cytochrome c oxidase from mammalian sources is not essential for its function in vitro.

Duke Scholars

Published In

Journal of inorganic biochemistry

DOI

EISSN

1873-3344

ISSN

0162-0134

Publication Date

March 1985

Volume

23

Issue

3-4

Start / End Page

365 / 372

Related Subject Headings

  • Ultracentrifugation
  • Structure-Activity Relationship
  • Sharks
  • Protons
  • Oxidation-Reduction
  • Myocardium
  • Muscles
  • Macromolecular Substances
  • Kinetics
  • Ion Channels
 

Citation

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Bickar, D., Lehninger, A., Brunori, M., Bonaventura, J., & Bonaventura, C. (1985). Functional equivalence of monomeric (shark) and dimeric (bovine) cytochrome c oxidase. Journal of Inorganic Biochemistry, 23(3–4), 365–372. https://doi.org/10.1016/0162-0134(85)85047-9
Bickar, D., A. Lehninger, M. Brunori, J. Bonaventura, and C. Bonaventura. “Functional equivalence of monomeric (shark) and dimeric (bovine) cytochrome c oxidase.Journal of Inorganic Biochemistry 23, no. 3–4 (March 1985): 365–72. https://doi.org/10.1016/0162-0134(85)85047-9.
Bickar D, Lehninger A, Brunori M, Bonaventura J, Bonaventura C. Functional equivalence of monomeric (shark) and dimeric (bovine) cytochrome c oxidase. Journal of inorganic biochemistry. 1985 Mar;23(3–4):365–72.
Bickar, D., et al. “Functional equivalence of monomeric (shark) and dimeric (bovine) cytochrome c oxidase.Journal of Inorganic Biochemistry, vol. 23, no. 3–4, Mar. 1985, pp. 365–72. Epmc, doi:10.1016/0162-0134(85)85047-9.
Bickar D, Lehninger A, Brunori M, Bonaventura J, Bonaventura C. Functional equivalence of monomeric (shark) and dimeric (bovine) cytochrome c oxidase. Journal of inorganic biochemistry. 1985 Mar;23(3–4):365–372.
Journal cover image

Published In

Journal of inorganic biochemistry

DOI

EISSN

1873-3344

ISSN

0162-0134

Publication Date

March 1985

Volume

23

Issue

3-4

Start / End Page

365 / 372

Related Subject Headings

  • Ultracentrifugation
  • Structure-Activity Relationship
  • Sharks
  • Protons
  • Oxidation-Reduction
  • Myocardium
  • Muscles
  • Macromolecular Substances
  • Kinetics
  • Ion Channels