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Medientyp: Sonstige Veröffentlichung; E-Artikel Titel: Structure and function of complex I in animals and plants – a comparative view Beteiligte: Senkler, Jennifer [VerfasserIn]; Senkler, Michael [VerfasserIn]; Braun, Hans-Peter [VerfasserIn] Erschienen: Oxford [u.a.] : Wiley-Blackwell, 2017 Erschienen in: Physiologia Plantarum 161 (2017), Nr. 1 ; Physiologia Plantarum Ausgabe: accepted Version Sprache: Englisch DOI: https://doi.org/10.15488/11654; https://doi.org/10.1111/ppl.12561 ISSN: 0031-9317 Schlagwörter: Models ; metabolism ; reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone) ; Molecular ; animal ; molecular model ; chemistry ; Plants ; mitochondrion ; cell membrane ; plant ; comparative study ; Mitochondria ; Electron Transport Complex I ; Animals Entstehung: Anmerkungen: Diese Datenquelle enthält auch Bestandsnachweise, die nicht zu einem Volltext führen. Beschreibung: The mitochondrial NADH dehydrogenase complex (complex I) has a molecular mass of about 1000 kDa and includes 40–50 subunits in animals, fungi and plants. It is composed of a membrane arm and a peripheral arm and has a conserved L-like shape in all species investigated. However, in plants and possibly some protists it has a second peripheral domain which is attached to the membrane arm on its matrix exposed side at a central position. The extra domain includes proteins resembling prokaryotic gamma-type carbonic anhydrases. We here present a detailed comparison of complex I from mammals and flowering plants. Forty homologous subunits are present in complex I of both groups of species. In addition, five subunits are present in mammalian complex I, which are absent in plants, and eight to nine subunits are present in plant complex I which do not occur in mammals. Based on the atomic structure of mammalian complex I and biochemical insights into complex I architecture from plants we mapped the species-specific subunits. Interestingly, four of the five animal-specific and five of the eight to nine plant-specific subunits are localized at the inner surface of the membrane arm of complex I in close proximity. We propose that the inner surface of the membrane arm represents a workbench for attaching proteins to complex I, which are not directly related to respiratory electron transport, like nucleoside kinases, acyl-carrier proteins or carbonic anhydrases. We speculate that further enzyme activities might be bound to this micro-location in other groups of organisms. © 2017 Scandinavian Plant Physiology Society Zugangsstatus: Freier Zugang