Journal Article

FZJ-2022-01888

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The respiratory supercomplex from C. glutamicum

Moe, A. ; Kovalova, T. ; Król, S. ; Yanofsky, D. J. ; Bott, M.FZJ* ; Sjöstrand, D. ; Rubinstein, J. L. (Corresponding author) ; Högbom, M. ; Brzezinski, P.

2022
Cell Press Cambridge, Mass.

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Please use a persistent id in citations: http://hdl.handle.net/2128/31015  doi:10.1016/j.str.2021.11.008

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.

Note: Biotechnologie 1

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Contributing Institute(s):

1. Biotechnologie (IBG-1)

Research Program(s):

1. 2171 - Biological and environmental resources for sustainable use (POF4-217) (POF4-217)

Appears in the scientific report 2022

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