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  Mechanistic and structural diversity between cytochrome bd isoforms of Escherichia coli

Grund, T. N., Radloff, M., Wu, D., Goojani, H. G., Witte, L. F., Jösting, W., et al. (2021). Mechanistic and structural diversity between cytochrome bd isoforms of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, 118(50): e2114013118. doi:10.1073/pnas.2114013118.

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Grund, Tamara N.1, Author              
Radloff, Melanie1, Author              
Wu, Di1, Author              
Goojani, Hojjat G.2, Author
Witte, Luca F.1, Author              
Jösting, Wiebke1, Author              
Buschmann, Sabine1, Author              
Müller, Hannelore1, Author              
Elamri, Isam3, Author
Welsch, Sonja4, Author              
Schwalbe, Harald3, Author
Michel, Hartmut1, Author              
Bald, Dirk2, Author
Safarian, Schara1, Author              
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Department of Molecular Cell Biology, Amsterdam Institute of Molecular and Life Sciences, Faculty of Science, Vrije Universiteit Amsterdam, 1081 HZ Amsterdam, The Netherlands, ou_persistent22              
3Center for Biomolecular Magnetic Resonance Institute of Organic Chemistry and Chemical Biology, Goethe Universität Frankfurt am Main, 60438 Frankfurt am Main, Germany, ou_persistent22              
4Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society, ou_3249263              


Free keywords: AppC; bd oxidase; microbiology; respiration; structural biology
 Abstract: The treatment of infectious diseases caused by multidrug-resistant pathogens is a major clinical challenge of the 21st century. The membrane-embedded respiratory cytochrome bd-type oxygen reductase is a critical survival factor utilized by pathogenic bacteria during infection, proliferation and the transition from acute to chronic states. Escherichia coli encodes for two cytochrome bd isoforms that are both involved in respiration under oxygen limited conditions. Mechanistic and structural differences between cydABX (Ecbd-I) and appCBX (Ecbd-II) operon encoded cytochrome bd variants have remained elusive in the past. Here, we demonstrate that cytochrome bd-II catalyzes oxidation of benzoquinols while possessing additional specificity for naphthoquinones. Our data show that although menaquinol-1 (MK1) is not able to directly transfer electrons onto cytochrome bd-II from E. coli, it has a stimulatory effect on its oxygen reduction rate in the presence of ubiquinol-1. We further determined cryo-EM structures of cytochrome bd-II to high resolution of 2.1 Å. Our structural insights confirm that the general architecture and substrate accessible pathways are conserved between the two bd oxidase isoforms, but two notable differences are apparent upon inspection: (i) Ecbd-II does not contain a CydH-like subunit, thereby exposing heme b595 to the membrane environment and (ii) the AppB subunit harbors a structural demethylmenaquinone-8 molecule instead of ubiquinone-8 as found in CydB of Ecbd-I Our work completes the structural landscape of terminal respiratory oxygen reductases of E. coli and suggests that structural and functional properties of the respective oxidases are linked to quinol-pool dependent metabolic adaptations in E. coli.


Language(s): eng - English
 Dates: 2021-07-302021-10-142021-12-14
 Publication Status: Published online
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.2114013118
PMID: 34873041
 Degree: -



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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : PNAS
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 118 (50) Sequence Number: e2114013118 Start / End Page: - Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230