Proteomic approach to characterize mitochondrial complex I from plants

authored by: Jennifer Klodmann, Hans Peter Braun
Abstract: Mitochondrial NADH dehydrogenase complex (complex I) is by far the largest protein complex of the respiratory chain. It is best characterized for bovine mitochondria and known to consist of 45 different subunits in this species. Proteomic analyses recently allowed for the first time to systematically explore complex I from plants. The enzyme is especially large and includes numerous extra subunits. Upon subunit separation by various gel electrophoresis procedures and protein identifications by mass spectrometry, overall 47 distinct types of proteins were found to form part of Arabidopsis complex I. An additional subunit, ND4L, is present but could not be detected by the procedures employed due to its extreme biochemical properties. Seven of the 48 subunits occur in pairs of isoforms, six of which were experimentally proven. Fifteen subunits of complex I from Arabidopsis are specific for plants. Some of these resemble enzymes of known functions, e.g. carbonic anhydrases and l-galactono-1,4-lactone dehydrogenase (GLDH), which catalyzes the last step of ascorbate biosynthesis. This article aims to review proteomic data on the protein composition of complex I in plants. Furthermore, a proteomic re-evaluation on its protein constituents is presented.
Organisation(s): Institute of Plant Genetics
Type: Article
Journal: PHYTOCHEMISTRY
Volume: 72
Pages: 1071-1080
No. of pages: 10
ISSN: 0031-9422
Publication date: 15.12.2010
Publication status: Published
Peer reviewed: Yes
ASJC Scopus subject areas: Biochemistry, Molecular Biology, Plant Science, Horticulture
Electronic version(s): https://doi.org/10.1016/j.phytochem.2010.11.012 (Access: Unknown)