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@ARTICLE{Moe:907200,
author = {Moe, Agnes and Kovalova, Terezia and Król, Sylwia and
Yanofsky, David J. and Bott, Michael and Sjöstrand, Dan and
Rubinstein, John L. and Högbom, Martin and Brzezinski,
Peter},
title = {{T}he respiratory supercomplex from {C}. glutamicum},
journal = {Structure},
volume = {30},
number = {3},
issn = {0969-2126},
address = {Cambridge, Mass.},
publisher = {Cell Press},
reportid = {FZJ-2022-01888},
pages = {338 - 349.e3},
year = {2022},
note = {Biotechnologie 1},
abstract = {Corynebacterium glutamicum is a preferentially aerobic
gram-positive bacterium belonging to the phylum
Actinobacteria, which also includes the pathogen
Mycobacterium tuberculosis. In these bacteria, respiratory
complexes III and IV form a CIII2CIV2 supercomplex that
catalyzes oxidation of menaquinol and reduction of dioxygen
to water. We isolated the C. glutamicum supercomplex and
used cryo-EM to determine its structure at 2.9 Å
resolution. The structure shows a central CIII2 dimer
flanked by a CIV on two sides. A menaquinone is bound in
each of the QN and QP sites in each CIII and an additional
menaquinone is positioned ∼14 Å from heme bL. A di-heme
cyt. cc subunit electronically connects each CIII with an
adjacent CIV, with the Rieske iron-sulfur protein positioned
with the iron near heme bL. Multiple subunits interact to
form a convoluted sub-structure at the cytoplasmic side of
the supercomplex, which defines a path for proton transfer
into CIV.},
cin = {IBG-1},
ddc = {540},
cid = {I:(DE-Juel1)IBG-1-20101118},
pnm = {2171 - Biological and environmental resources for
sustainable use (POF4-217)},
pid = {G:(DE-HGF)POF4-2171},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:34910901},
UT = {WOS:000766494300005},
doi = {10.1016/j.str.2021.11.008},
url = {https://juser.fz-juelich.de/record/907200},
}