Details
| Original language | English |
|---|---|
| Pages (from-to) | 1071-1080 |
| Number of pages | 10 |
| Journal | PHYTOCHEMISTRY |
| Volume | 72 |
| Issue number | 10 |
| Publication status | Published - 15 Dec 2010 |
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.
Keywords
- Arabidopsis thaliana, Carbonic anhydrase, Complex I, Mitochondria, NADH dehydrogenase, Respiratory chain
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Agricultural and Biological Sciences(all)
- Plant Science
- Agricultural and Biological Sciences(all)
- Horticulture
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In: PHYTOCHEMISTRY, Vol. 72, No. 10, 15.12.2010, p. 1071-1080.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Proteomic approach to characterize mitochondrial complex I from plants
AU - Klodmann, Jennifer
AU - Braun, Hans Peter
N1 - Funding information: This work was supported by the Deutsche Forschungsgemeinschaft (DFG), Grants Br1829/8-1 and Br1829/10-1.
PY - 2010/12/15
Y1 - 2010/12/15
N2 - 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.
AB - 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.
KW - Arabidopsis thaliana
KW - Carbonic anhydrase
KW - Complex I
KW - Mitochondria
KW - NADH dehydrogenase
KW - Respiratory chain
UR - http://www.scopus.com/inward/record.url?scp=79958144995&partnerID=8YFLogxK
U2 - 10.1016/j.phytochem.2010.11.012
DO - 10.1016/j.phytochem.2010.11.012
M3 - Article
C2 - 21167537
AN - SCOPUS:79958144995
VL - 72
SP - 1071
EP - 1080
JO - PHYTOCHEMISTRY
JF - PHYTOCHEMISTRY
SN - 0031-9422
IS - 10
ER -