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The Rate and Coupling Efficiency of Oxidative Phosphorylation in Mitochondria and Cells
Guest Speaker:
Dr. Martin Brand
Professor, Buck Institute
Novato, CA US
MRC Dunn Human Nutrition Unit, Cambridge, UK
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
View On-Demand Webinar*
December 8, 2008
11:00am EST
Event ID#127397
Guest Speaker Contact Information:
Dr. Martin Brand
Professor, Buck Institute, Novato, CA US
MRC Dunn Human Nutrition Unit, Cambridge, UK
Email: Mbrand@buckinstitute.org
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.
*None of the content on this website should be considered medical or psychological advice. Seahorse Biosciences does not give medical advice or diagnose medical and psychological conditions. Although every effort is made to assure that information on this site is accurate and current, knowledge in the field of cellular bioenergetics is growing rapidly and all data is subject to change without notice.
You should consult with your healthcare professional for specific advice relating to your medical questions or conditions. None of the information, statements and/or links contained on the website are intended to replace the attention or medical instructions from a healthcare professional. Only your practitioner can completely and appropriately assess your situation and make conclusive decisions regarding your care.
