Native MS of membrane-embedded
protein complexes analyzed directly
from their native environment. Regions of the mass spectrum recorded
for inner membranes from E. coli yield
cytochromes, the Ton complex multidrug transporters, and the intact
ATP synthase in complex with the SecYEG translocon. (A, B) Expanded
regions of the spectrum assigned to cytochrome bo3 and cytochrome bd oxidase, showing
peak splitting due to binding of quinol and heme groups. The pentameric
ExbB complex (with one copy of ExbD in the center of the pore) that
forms part of the TonB complex is also observed (yellow). (C) High-m/z region of the mass spectrum assigned
to the multidrug efflux pumps AcrAB and MdtAB and the intact ATP synthase.
Expansion of peaks assigned to the ATPase reveals binding of the SecY
(blue), SecYG (green), and SecYEG (orange) charge states 52+, 53+,
and 54+. Complexes observed in mass spectra are shown schematically,
with subunits that have dissociated shown in gray. Reproduced with
permission from ref (323). Copyright 2018 Chorev et al.