The Oxidative Phosphorylation system of the mitochondria in plants

Originalpublikation

Braun, H.-P.: The Oxidative Phosphorylation system of the mitochondria in plants. In: Mitochondrion 53 (2020), S. 66-75. DOI: https://doi.org/10.1016/j.mito.2020.04.007

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Zusammenfassung:
Mitochondrial Oxidative Phosphorylation (OXPHOS) provides ATP for driving cellular functions. In plants, OXPHOS takes place in the context of photosynthesis. Indeed, metabolism of mitochondria and chloroplasts is tightly linked. OXPHOS has several extra functions in plants. This review takes a view on the OXPHOS system of plants, the electron transfer chain (ETC), the ATP synthase complex and the numerous supplementary enzymes involved. Electron transport pathways are especially branched in plants. Furthermore, the “classical” OXPHOS complexes include extra subunits, some of which introduce side activities into these complexes. Consequently, and to a remarkable degree, OXPHOS is a multi-functional system in plants that needs to be efficiently regulated with respect to all its physiological tasks in the mitochondria, the chloroplasts, and beyond. Regulatory mechanisms based on posttranslational protein modifications and formation of supramolecular protein assemblies are summarized and discussed.
Lizenzbestimmungen: CC BY-NC-ND 4.0 Unported - https://creativecommons.org/licenses/by-nc-nd/4.0/
Publikationstyp: Article
Publikationsstatus: publishedVersion
Erstveröffentlichung: 2020
Schlagwörter (englisch): Arabidopsis thaliana, ATP synthase, Electron transfer chain, Gamma-type carbonic anhydrase, NADH dehydrogenase, Oxidative phosphorylation, Photosynthesis, Plant mitochondria, Respiratory protein complexes, Respiratory supercomplexes, alternative NAD(P)H dehydrogenase, carbonate dehydratase I, carbonate dehydratase II, carbonate dehydratase III, complex V, cytochrome c, cytochrome c oxidase, electron transfer flavoprotein ubiquinone oxidoreductase, electron transferring flavoprotein, levo galactono 1,4 lactone dehydrogenase, oxidoreductase, proline dehydrogenase, proton transporting adenosine triphosphate synthase, reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone), succinate dehydrogenase (ubiquinone), ubiquinol cytochrome c reductase, unclassified drug, mitochondrial protein, plant protein, amino acid sequence, Arabidopsis thaliana, biochemical analysis, chemical composition, citric acid cycle, cryoelectron microscopy, electron microscopy, electron transport, enzyme regulation, enzyme structure, mass spectrometry, mitochondrial respiration, mitochondrion, native polyacrylamide gel electrophoresis, nonhuman, oxidative phosphorylation, photorespiration, photosynthesis, plant physiology, priority journal, protein assembly, protein processing, regulatory mechanism, Review, single particle cryoelectron microscopy, single particle electron microscopy, X ray crystallography, chloroplast, metabolism, mitochondrion, plant, Chloroplasts, Electron Transport, Mitochondria, Mitochondrial Proteins, Oxidative Phosphorylation, Photosynthesis, Plant Proteins, Plants, Protein Processing, Post-Translational
Fachliche Zuordnung (DDC): 540 | Chemie

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