scholarly journals Hybrid Clear/Blue Native Electrophoresis for the Separation and Analysis of Mitochondrial Respiratory Chain Supercomplexes

10.3791/59294 ◽  
2019 ◽  
Author(s):  
Alexanne Cuillerier ◽  
Yan Burelle
Keyword(s):  
Respiratory Chain ◽  
Mitochondrial Respiratory Chain ◽  
Native Electrophoresis ◽  
Blue Native Electrophoresis ◽  
Blue Native ◽  
Mitochondrial Respiratory

scholarly journals Kinetics of integrated electron transfer in the mitochondrial respiratory chain: random collisions vs. solid state electron channeling

2007 ◽  
Vol 292 (4) ◽  
pp. C1221-C1239 ◽  
Author(s):  
Giorgio Lenaz ◽  
Maria Luisa Genova
Keyword(s):  
Respiratory Chain ◽  
Coenzyme Q ◽  
Lateral Diffusion ◽  
Kinetic Studies ◽  
Mitochondrial Respiratory Chain ◽  
Substrate Channeling ◽  
Solid State Electron ◽  
Native Electrophoresis ◽  
Redox Molecules ◽  
Mitochondrial Respiratory

Recent evidence, mainly based on native electrophoresis, has suggested that the mitochondrial respiratory chain is organized in the form of supercomplexes, due to the aggregation of the main respiratory chain enzymatic complexes. This evidence strongly contrasts the previously accepted model, the Random Diffusion Model, largely based on kinetic studies, stating that the complexes are randomly distributed in the lipid bilayer of the inner membrane and functionally connected by lateral diffusion of small redox molecules, i.e., coenzyme Q and cytochrome c. This review critically examines the experimental evidence, both structural and functional, pertaining to the two models and attempts to provide an updated view of the organization of the respiratory chain and of its kinetic consequences. The conclusion that structural respiratory assemblies exist is overwhelming, whereas the expected functional consequence of substrate channeling between the assembled enzymes is controversial. Examination of the available evidence suggests that, although the supercomplexes are structurally stable, their kinetic competence in substrate channeling is more labile and may depend on the system under investigation and the assay conditions.

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