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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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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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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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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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Related Experiment Video

Updated: Mar 20, 2026

Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights
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The MICOS complex of human mitochondria.

Vera Kozjak-Pavlovic1

  • 1Biocenter, Chair of Microbiology, University of Würzburg, Am Hubland, 97074, Würzburg, Germany. Vera.Kozjak@uni-wuerzburg.de.

Cell and Tissue Research
|June 2, 2016
PubMed
Summary

The mitochondrial contact site and cristae organizing system (MICOS) is vital for mitochondrial cristae structure. This review details the human MICOS complex, its subunits, and future research directions.

Area of Science:

  • Cell Biology
  • Mitochondrial Biology
  • Biochemistry

Background:

  • Mitochondria, organelles of endosymbiotic origin, possess a double membrane structure.
  • The inner mitochondrial membrane invaginates into cristae, increasing surface area for function.
  • The mitochondrial contact site and cristae organizing system (MICOS) is essential for cristae formation and maintenance.

Purpose of the Study:

  • To summarize current knowledge of the human MICOS complex.
  • To detail the constituents of the human MICOS complex.
  • To discuss future research perspectives on MICOS in human mitochondria.

Main Methods:

  • Literature review of existing studies on the human MICOS complex.
  • Comparative analysis of human and yeast MICOS systems.
Keywords:
CristaeMIBMICOSMitochondriaSAM

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  • Identification and functional exploration of MICOS subunits.

    • Main Results:

    • The human MICOS complex displays greater complexity than its yeast counterpart.
    • Several MICOS subunits have been identified, but many functions remain uncharacterized.
    • MICOS plays a critical role in maintaining mitochondrial cristae structure and function.

    Conclusions:

    • The human MICOS complex is a key determinant of mitochondrial architecture.
    • Further research is needed to fully elucidate the function of all MICOS subunits.
    • Understanding MICOS is crucial for advancing mitochondrial biology and disease research.