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Related Concept Videos

The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

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The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
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Electron Transport Chain: Complex I and II01:46

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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
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The Supercomplexes in the Crista Membrane01:41

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The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
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Chemiosmosis01:32

Chemiosmosis

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Oxidative phosphorylation is a highly efficient process that generates large amounts of adenosine triphosphate (ATP), the basic unit of energy that drives many cellular processes. Oxidative phosphorylation involves two processes— the electron transport chain and chemiosmosis.
Electron Transport Chain
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Electron Transport Chain: Complex III and IV01:43

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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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ATP Synthase: Mechanism01:48

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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Related Experiment Video

Updated: May 9, 2025

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

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Cryo-EM of Mitochondrial Complex I and ATP Synthase.

Werner Kühlbrandt1, Luis A M Carreira1, Özkan Yildiz1

  • 1Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany;

Annual Review of Biophysics
|May 6, 2025
PubMed
Summary
This summary is machine-generated.

Recent cryo-electron microscopy (cryo-EM) studies reveal high-resolution structures of mitochondrial complex I and ATP synthase. These findings illuminate functional states and proton transfer mechanisms in these vital protein complexes.

Keywords:
ATP synthasecomplex Icryo-electron microscopycryo-electron tomographymitochondriarespiratory chain

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Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
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Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution
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Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
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Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Mitochondrial complex I and ATP synthase are crucial for cellular energy production.
  • Understanding their structure is key to elucidating energy transduction mechanisms.
  • Cryo-electron microscopy (cryo-EM) offers high-resolution insights into membrane protein complexes.

Purpose of the Study:

  • To review recent advancements in cryo-EM for studying mitochondrial complex I and ATP synthase.
  • To highlight structural insights into the functional states and mechanisms of these complexes.
  • To discuss the potential of cryo-EM techniques for in situ structural determination.

Main Methods:

  • Single-particle cryo-electron microscopy (cryo-EM) was employed to determine high-resolution structures.
  • Cryo-electron tomography and subtomogram averaging were explored for in situ analysis.
  • Analysis focused on structural variations and conformational changes related to function.

Main Results:

  • High-resolution (up to 2 Å) cryo-EM structures of complex I revealed distinct functional states.
  • Observed changes include loop conformations near the Q binding site and internal water clusters.
  • Cryo-EM structures of ATP synthase dimers showed various rotary states (2.7–3.5 Å resolution).

Conclusions:

  • Recent cryo-EM studies provide unprecedented structural detail of mitochondrial complex I and ATP synthase.
  • These structures advance the understanding of their molecular mechanisms and proton transfer pathways.
  • Cryo-EM techniques hold significant promise for future in situ structural biology investigations.