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Clarifying the supercomplex: the higher-order organization of the mitochondrial electron transport chain
by
Letts, James A
, Sazanov, Leonid A
in
101/28
/ 101/58
/ 631/45/173
/ 631/535/1258/1259
/ 64
/ 82
/ 82/83
/ Analysis
/ Biochemistry
/ Biological Microscopy
/ Cryoelectron Microscopy
/ Dimers
/ Electron Transport
/ Electron transport chain
/ Electron Transport Chain Complex Proteins - chemistry
/ Electron Transport Chain Complex Proteins - metabolism
/ Electrons
/ Food
/ Life Sciences
/ Membrane Biology
/ Mitochondria
/ Mitochondria - enzymology
/ Mitochondria - metabolism
/ Oxidation
/ Oxidative Phosphorylation
/ Phosphorylation
/ Properties
/ Protein Multimerization
/ Protein Structure
/ review-article
2017
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Clarifying the supercomplex: the higher-order organization of the mitochondrial electron transport chain
by
Letts, James A
, Sazanov, Leonid A
in
101/28
/ 101/58
/ 631/45/173
/ 631/535/1258/1259
/ 64
/ 82
/ 82/83
/ Analysis
/ Biochemistry
/ Biological Microscopy
/ Cryoelectron Microscopy
/ Dimers
/ Electron Transport
/ Electron transport chain
/ Electron Transport Chain Complex Proteins - chemistry
/ Electron Transport Chain Complex Proteins - metabolism
/ Electrons
/ Food
/ Life Sciences
/ Membrane Biology
/ Mitochondria
/ Mitochondria - enzymology
/ Mitochondria - metabolism
/ Oxidation
/ Oxidative Phosphorylation
/ Phosphorylation
/ Properties
/ Protein Multimerization
/ Protein Structure
/ review-article
2017
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Clarifying the supercomplex: the higher-order organization of the mitochondrial electron transport chain
by
Letts, James A
, Sazanov, Leonid A
in
101/28
/ 101/58
/ 631/45/173
/ 631/535/1258/1259
/ 64
/ 82
/ 82/83
/ Analysis
/ Biochemistry
/ Biological Microscopy
/ Cryoelectron Microscopy
/ Dimers
/ Electron Transport
/ Electron transport chain
/ Electron Transport Chain Complex Proteins - chemistry
/ Electron Transport Chain Complex Proteins - metabolism
/ Electrons
/ Food
/ Life Sciences
/ Membrane Biology
/ Mitochondria
/ Mitochondria - enzymology
/ Mitochondria - metabolism
/ Oxidation
/ Oxidative Phosphorylation
/ Phosphorylation
/ Properties
/ Protein Multimerization
/ Protein Structure
/ review-article
2017
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Clarifying the supercomplex: the higher-order organization of the mitochondrial electron transport chain
Journal Article
Clarifying the supercomplex: the higher-order organization of the mitochondrial electron transport chain
2017
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Overview
Five protein complexes, CI–CV, form the oxidative phosphorylation electron transport chain in the mitochondrial membrane and can be found organized into supercomplexes (SCs): I+III2+IV, or respirasome; I+III2; III2+IV; and CV2. Letts and Sazanov review current knowledge on the structure, assembly and function of respiratory SCs.
The oxidative phosphorylation electron transport chain (OXPHOS-ETC) of the inner mitochondrial membrane is composed of five large protein complexes, named CI–CV. These complexes convert energy from the food we eat into ATP, a small molecule used to power a multitude of essential reactions throughout the cell. OXPHOS-ETC complexes are organized into supercomplexes (SCs) of defined stoichiometry: CI forms a supercomplex with CIII
2
and CIV (SC I+III
2
+IV, known as the respirasome), as well as with CIII
2
alone (SC I+III
2
). CIII
2
forms a supercomplex with CIV (SC III
2
+IV) and CV forms dimers (CV
2
). Recent cryo-EM studies have revealed the structures of SC I+III
2
+IV and SC I+III
2
. Furthermore, recent work has shed light on the assembly and function of the SCs. Here we review and compare these recent studies and discuss how they have advanced our understanding of mitochondrial electron transport.
Publisher
Nature Publishing Group US,Nature Publishing Group
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