Difference between revisions of "Moore 2017 MiPschool Obergurgl"
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{{Abstract | {{Abstract | ||
|title=[[File:Moore Anthony L.jpg|left|90px|Anthony Moore]] | |title=[[File:Moore Anthony L.jpg|left|90px|Anthony Moore]] The electron transfer system – Q redox regulation and mitochondrial pathways to oxygen. | ||
|info=[[MITOEAGLE]] | |info=[[MITOEAGLE]] | ||
|authors=Moore AL | |authors=Moore AL | ||
Revision as of 15:21, 19 July 2017
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Link: MITOEAGLE
Moore AL (2017)
Event: MiPschool Obergurgl 2017
The mitochondrial respiratory chain is comprised of the NADH dehydrogenase, succinate dehydrogenase, the cytochrome bc1 complex and cytochrome c oxidase all of which are multi-enzyme complexes that are randomly distributed within the inner mitochondrial membrane. Since the respiratory chain complexes are randomly distributed within the membrane and are at differing stoichiometries with respect to Complex I, the rate of electron transport is governed by the mobility and redox state of ubiquinone and cytochrome c respectively. In this talk I will discuss evidence in favour of a homogenous Q-pool the redox state of which governs the rate of electron transport. I will also discuss deviations form Q-pool behaviour, its role within supercomplexes and how Q deficiencies can cause mitochondrial respiratory diseases and finally novel techniques for the measurement of Q-pool redox poise using ‘Q-electrodes’.
• Bioblast editor: Kandolf G
Labels: MiParea: Respiration
Enzyme: Complex II;succinate dehydrogenase
Event: A1, Review
Affiliations
- Biochem Medicine, School Life Sciences, Univ Sussex, Brighton, United Kindgdom.- [email protected]
