Journal
PLANT CELL
Volume 33, Issue 6, Pages 2072-2091Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/plcell/koab092
Keywords
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Funding
- Max Planck Society
- Deutsche Forschungsgemeinschaft [BR 1829/10-2, SFB 807]
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Mitochondrial complex I is the main site for electron transfer and proton gradient generation. It is composed of two arms and a bridge domain, with different conformations and angles potentially regulating its activity.
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 angstrom resolution. In both complexes, a heterotrimeric gamma-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.
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