Details
| Original language | English |
|---|---|
| Pages (from-to) | 2072-2091 |
| Number of pages | 20 |
| Journal | Plant Cell |
| Volume | 33 |
| Issue number | 6 |
| Early online date | 26 Mar 2021 |
| Publication status | Published - Jun 2021 |
Abstract
Mitochondrial complex I is the main site for electron transfer to the respiratory chain and generates much of the proton gradient across the inner mitochondrial membrane. Complex I is composed of two arms, which form a conserved L-shape. We report the structures of the intact, 47-subunit mitochondrial complex I from Arabidopsis thaliana and the 51-subunit complex I from the green alga Polytomella sp., both at around 2.9 Å resolution. In both complexes, a heterotrimeric c-carbonic anhydrase domain is attached to the membrane arm on the matrix side. Two states are resolved in A. thaliana complex I, with different angles between the two arms and different conformations of the ND1 (NADH dehydrogenase subunit 1) loop near the quinol binding site. The angle appears to depend on a bridge domain, which links the peripheral arm to the membrane arm and includes an unusual ferredoxin. We propose that the bridge domain participates in regulating the activity of plant complex I.
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Plant Science
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: Plant Cell, Vol. 33, No. 6, 06.2021, p. 2072-2091.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - A ferredoxin bridge connects the two arms of plant mitochondrial complex I
AU - Klusch, Niklas
AU - Senkler, Jennifer
AU - Yildiz, Özkan
AU - Kühlbrandt, Werner
AU - Braun, Hans-Peter
N1 - Funding Information: This work was funded by the Max Planck Society (W.K., Ö.Y., and N.K.) and by the Deutsche Forschungsgemeinschaft (grant BR 1829/10-2—H.P.B. and J.S.; SFB 807—W.K. and N.K.).
PY - 2021/6
Y1 - 2021/6
N2 - Mitochondrial complex I is the main site for electron transfer to the respiratory chain and generates much of the proton gradient across the inner mitochondrial membrane. Complex I is composed of two arms, which form a conserved L-shape. We report the structures of the intact, 47-subunit mitochondrial complex I from Arabidopsis thaliana and the 51-subunit complex I from the green alga Polytomella sp., both at around 2.9 Å resolution. In both complexes, a heterotrimeric c-carbonic anhydrase domain is attached to the membrane arm on the matrix side. Two states are resolved in A. thaliana complex I, with different angles between the two arms and different conformations of the ND1 (NADH dehydrogenase subunit 1) loop near the quinol binding site. The angle appears to depend on a bridge domain, which links the peripheral arm to the membrane arm and includes an unusual ferredoxin. We propose that the bridge domain participates in regulating the activity of plant complex I.
AB - Mitochondrial complex I is the main site for electron transfer to the respiratory chain and generates much of the proton gradient across the inner mitochondrial membrane. Complex I is composed of two arms, which form a conserved L-shape. We report the structures of the intact, 47-subunit mitochondrial complex I from Arabidopsis thaliana and the 51-subunit complex I from the green alga Polytomella sp., both at around 2.9 Å resolution. In both complexes, a heterotrimeric c-carbonic anhydrase domain is attached to the membrane arm on the matrix side. Two states are resolved in A. thaliana complex I, with different angles between the two arms and different conformations of the ND1 (NADH dehydrogenase subunit 1) loop near the quinol binding site. The angle appears to depend on a bridge domain, which links the peripheral arm to the membrane arm and includes an unusual ferredoxin. We propose that the bridge domain participates in regulating the activity of plant complex I.
UR - http://www.scopus.com/inward/record.url?scp=85105935489&partnerID=8YFLogxK
U2 - 10.1101/2020.11.23.393975
DO - 10.1101/2020.11.23.393975
M3 - Article
C2 - 33768254
VL - 33
SP - 2072
EP - 2091
JO - Plant Cell
JF - Plant Cell
SN - 1040-4651
IS - 6
ER -