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The bridge-like connection formed by the complex I domains 5/6 on the matrix arm and the PMP/CMP on the membrane arm appears thicker in the supercomplex than in the isolated complex I (Clason et al, 2010).
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His already iffy arm appears to be getting weaker.
CIII form a dimer in the respirasome, located at concave side of CI's membrane arm.
All these structures show the intact structure of CI to be L-shaped, with a matrix arm and a membrane arm.
The central TMHs of NDUFA11 bundle together and parallel the TMH domain of CI's membrane arm.
Electron microscopy revealed the two-part structure of the complex with a peripheral arm involved in electron transfer and a membrane arm most likely involved in proton translocation.
The L-shaped complex consists of a hydrophilic arm, where electron transfer occurs, and a membrane arm, where proton translocation takes place.
It consists of a peripheral arm harbouring all known redox active prosthetic groups and a membrane arm with a yet unknown number of proton translocation sites.
Most likely, proton translocation in the membrane arm is enabled by the energy of the electron transfer reaction in the peripheral arm transmitted by conformational changes.
When compared with CI in the free form, the matrix arm of CI and the distal end of CI's membrane arm bend a little towards the central part of CI's membrane arm in the respirasome, to better interact with CIII and CIV.
Finally, subcomplex E contained at least subunits NDUFC2 and MTND4, also members of the membrane arm.
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