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Mitochondrial respiration

Super-complex supercomplex

Nature Plants volume 9, pages 5–6 (2023)Cite this article

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In plant mitochondria, NADH dehydrogenase (complex I) and the cytochrome bc1 complex (complex III) form a I + III2 supercomplex, which is thought to stabilize the structure of the component complexes. Protein–protein interactions at three sites on the membrane arm of complex I partly resemble those in mammals, but also have plant-specific features.

In most eukaryotic cells, the electron transport chain (ETC) in the inner mitochondrial membrane (IMM) transports electrons mainly from NADH, produced in the Krebs cycle, to oxygen. This electron transport, mediated by four multisubunit protein complexes, is coupled to proton pumping to create an electrochemical proton gradient across the IMM, which is used by ATP synthase to make ATP1. A variety of supercomplexes is formed depending on the specific conditions, although their precise functions are unknown. The structure of one of these, the mammalian I + III2 supercomplex, has already been determined2. Plant mitochondria contain the same four ETC complexes as mammals, but the compositions of especially complexes I and III (CI and CIII) differ in a number of ways from their mammalian counterparts3. In this issue of Nature Plants, Klusch et al.4 and Maldonado et al.5 both report the cryo-electron microscope structure of a plant I + III2 supercomplex: the former from Arabidopsis at 2.0 Å resolution and the latter from bean at 3.2 Å resolution.

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Fig. 1: The overall structure of two I + III2 supercomplexes.

References

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  1. Department of Molecular Biology and Genetics, Aarhus University, Slagelse, Denmark

    Ian Max Møller

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  1. Ian Max Møller
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Correspondence to Ian Max Møller.

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Møller, I.M. Super-complex supercomplex. Nat. Plants 9, 5–6 (2023). https://doi.org/10.1038/s41477-022-01329-1

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