Seahorse Bioscience

The Rate and Coupling Efficiency of Oxidative Phosphorylation in Mitochondria and Cells

Dr. Martin Brand
Guest Speaker:
Dr. Martin Brand
Professor, Buck Institute
Novato, CA US
MRC Dunn Human Nutrition Unit, Cambridge, UK

Webinar Abstract:

During oxidative phosphorylation, oxidation of substrates is coupled to phosphorylation of ADP to ATP. Mitochondria pump out protons to build up a protonmotive force, which is then used to drive protons back through the ATP synthase, generating ATP. However, some protons leak back across the membrane, lowering the coupling efficiency.

There are differences in the kinetics of the components of oxidative phosphorylation, depending on genetic makeup, signaling pathways, oxidative stress and disease, or the application of pharmacological or toxic compounds. These differences can alter steady-state rates, coupling efficiencies and the response to energy demand.

A set of theoretical and experimental techniques has been developed to resolve these differences and identify their primary sites of action on the bioenergetics of mitochondria and cells.

Join us for this 45-minute webinar as we discuss:

  • Coupling efficiency in mitochondria and cells
  • Modular kinetic analysis of the primary sites of action of effectors that change oxidative phosphorylation
  • Effects of mitochondrial haplogroup on oxidative phosphorylation and coupling efficiency in human cybrid cells
  • Effects of uncoupling protein 2 on oxidative phosphorylation and coupling efficiency in a pancreatic beta cell model

Assay:

Mitochondrial Function: Coupling efficiency (Ologo, ATP turnover)/BOFA

 

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Originally presented December 8, 2008

Selected Publications


1. Brand, M. D., Pakay, J. L., Ocloo, A., Kokoszka, J., Wallace, D. C., Brookes, P. S. & Cornwall, E. J. (2005). The basal proton conductance of mitochondria depends on adenine nucleotide translocase content. Biochem. J. 392, 353-362.

2. Brand, M. D. & Esteves, T. C. (2005). Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3. Cell Metab. 2, 85-93.

3. Lambert, A. J. & Brand, M. D. (2004). Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane. Biochem. J. 382, 511-517.

4. Echtay, K. S., Esteves, T. C., Pakay, J. L., Jekabsons, M. B., Lambert, A. J., Portero-Otín, M., Pamplona, R., Vidal-Puig, A. J., Wang, S., Roebuck, S. J. & Brand, M. D. (2003). A signalling role for 4-hydroxy-2-nonenal in regulation of mitochondrial uncoupling. EMBO J. 22, 4103-4110.