Homologous bd oxidases share the same architecture but differ in mechanism

Alexander Theßeling, Tim Rasmussen, Sabrina Burschel, Daniel Wohlwend, Jan Kägi, Rolf Müller, Bettina Böttcher and Thorsten Friedrich ()
Additional contact information
Alexander Theßeling: Albert-Ludwigs-Universität
Tim Rasmussen: Julius-Maximilians-Universität
Sabrina Burschel: Albert-Ludwigs-Universität
Daniel Wohlwend: Albert-Ludwigs-Universität
Jan Kägi: Albert-Ludwigs-Universität
Rolf Müller: Helmholtz Centre for Infection Research and Department of Pharmacy at Saarland University
Bettina Böttcher: Julius-Maximilians-Universität
Thorsten Friedrich: Albert-Ludwigs-Universität

Nature Communications, 2019, vol. 10, issue 1, 1-7

Abstract: Abstract Cytochrome bd oxidases are terminal reductases of bacterial and archaeal respiratory chains. The enzyme couples the oxidation of ubiquinol or menaquinol with the reduction of dioxygen to water, thus contributing to the generation of the protonmotive force. Here, we determine the structure of the Escherichia coli bd oxidase treated with the specific inhibitor aurachin by cryo-electron microscopy (cryo-EM). The major subunits CydA and CydB are related by a pseudo two fold symmetry. The heme b and d cofactors are found in CydA, while ubiquinone-8 is bound at the homologous positions in CydB to stabilize its structure. The architecture of the E. coli enzyme is highly similar to that of Geobacillus thermodenitrificans, however, the positions of heme b595 and d are interchanged, and a common oxygen channel is blocked by a fourth subunit and substituted by a more narrow, alternative channel. Thus, with the same overall fold, the homologous enzymes exhibit a different mechanism.

Date: 2019
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-019-13122-4 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13122-4

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-019-13122-4

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().