The respiratory supercomplex from C. glutamicum

Agnes Moe; Terezia Kovalova; Sylwia Król; David J Yanofsky; Michael Bott; Dan Sjöstrand; John L Rubinstein; Martin Högbom; Peter Brzezinski

doi:10.1016/j.str.2021.11.008

The respiratory supercomplex from C. glutamicum

Structure. 2022 Mar 3;30(3):338-349.e3. doi: 10.1016/j.str.2021.11.008. Epub 2021 Dec 14.

Authors

Agnes Moe¹, Terezia Kovalova¹, Sylwia Król¹, David J Yanofsky², Michael Bott³, Dan Sjöstrand¹, John L Rubinstein⁴, Martin Högbom⁵, Peter Brzezinski⁶

Affiliations

¹ Department of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, 106 91 Stockholm, Sweden.
² Molecular Medicine Program, The Hospital for Sick Children, 686 Bay Street, Toronto, ON M5G 0A4, Canada; Department of Medical Biophysics, The University of Toronto, 101 College Street, Toronto, ON M5G 1L7, Canada.
³ Institute of Bio- and Geosciences, IBG-1: Biotechnology, Forschungszentrum Jülich, 52425 Jülich, Germany.
⁴ Molecular Medicine Program, The Hospital for Sick Children, 686 Bay Street, Toronto, ON M5G 0A4, Canada; Department of Medical Biophysics, The University of Toronto, 101 College Street, Toronto, ON M5G 1L7, Canada; Department of Biochemistry, The University of Toronto, 1 Kings College Circle, Toronto, ON M5S 1A8, Canada. Electronic address: john.rubinstein@utoronto.ca.
⁵ Department of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, 106 91 Stockholm, Sweden. Electronic address: martin.hogbom@dbb.su.se.
⁶ Department of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, 106 91 Stockholm, Sweden. Electronic address: peter.brzezinski@dbb.su.se.

PMID: 34910901
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 Q_N and Q_P sites in each CIII and an additional menaquinone is positioned ∼14 Å from heme b_L. 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 b_L. 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.

Keywords: Actinobacteria; Bioenergetics; Electron transfer; cytochrome bc(1); cytochrome c oxidase; electrochemical potential; energy conservation; membrane protein; proton transfer; respiration.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Electron Transport
Electron Transport Complex IV* / chemistry
Heme*
Mitochondrial Membranes / metabolism
Oxidation-Reduction
Vitamin K 2 / metabolism

Substances

Vitamin K 2
Heme
Electron Transport Complex IV

Grants and funding

PJT162186 /CIHR/Canada