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Updated: Mar 6, 2026

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
Published on: July 20, 2022
Structure and function of complex I in animals and plants - a comparative view.
Jennifer Senkler1, Michael Senkler1, Hans-Peter Braun1
1Institut für Pflanzengenetik, Leibniz Universität Hannover, Hannover, 30419, Germany.
Mitochondrial complex I in mammals and plants shares core subunits but differs in species-specific ones. These unique subunits, particularly in plants, are located on the membrane arm, suggesting a role beyond respiratory electron transport.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Respiration
Background:
- Mitochondrial NADH dehydrogenase (complex I) is a large enzyme complex crucial for cellular respiration.
- Complex I has a conserved structure across eukaryotes but exhibits variations, especially in plants.
- Plant complex I possesses an additional peripheral domain with potential novel functions.
Purpose of the Study:
- To compare the subunit composition of complex I between mammals and flowering plants.
- To identify species-specific subunits and map their locations within the complex.
- To investigate the functional implications of these species-specific subunits.
Main Methods:
- Comparative analysis of complex I subunit composition in mammals and plants.
- Utilizing atomic structures of mammalian complex I and biochemical data from plants.
- Mapping of species-specific subunits onto the complex I structure.
Main Results:
- Complex I in mammals and plants shares 40 homologous subunits.
- Mammalian complex I has five unique subunits, while plant complex I has eight to nine unique subunits.
- Many species-specific subunits are localized to the inner surface of the membrane arm.
Conclusions:
- The inner surface of the complex I membrane arm acts as a platform for attaching non-respiratory proteins.
- Plant-specific subunits, including carbonic anhydrases, are associated with this platform.
- This suggests complex I may integrate additional enzymatic activities beyond electron transport.
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