A ferredoxin bridge connects the two arms of plant mitochondrial complex I

verfasst von

Niklas Klusch, Jennifer Senkler, Özkan Yildiz, Werner Kühlbrandt, Hans-Peter Braun

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.

Organisationseinheit(en)

Institut für Pflanzengenetik

Externe Organisation(en)

Max-Planck-Institut für Biophysik

Typ

Artikel

Journal

Plant Cell

Band

33

Seiten

2072-2091

Anzahl der Seiten

20

ISSN

1040-4651

Publikationsdatum

06.2021

Publikationsstatus

Veröffentlicht

Peer-reviewed

Ja

ASJC Scopus Sachgebiete

Pflanzenkunde, Zellbiologie

Elektronische Version(en)

https://doi.org/10.1101/2020.11.23.393975 (Zugang: Offen)
https://doi.org/10.1093/plcell/koab092 (Zugang: Offen)