A 2.2Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases

Flynn, Alex J, Antonyuk, Svetlana V ORCID: 0000-0002-2779-9946, Eady, Robert R, Muench, Stephen P and Hasnain, S Samar (2023) A 2.2Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases. NATURE COMMUNICATIONS, 14 (1). 3416-.

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Official URL: http://dx.doi.org/10.1038/s41467-023-39140-x

Abstract

Quinol-dependent nitric oxide reductases (qNORs) are considered members of the respiratory heme-copper oxidase superfamily, are unique to bacteria, and are commonly found in pathogenic bacteria where they play a role in combating the host immune response. qNORs are also essential enzymes in the denitrification pathway, catalysing the reduction of nitric oxide to nitrous oxide. Here, we determine a 2.2 Å cryoEM structure of qNOR from Alcaligenes xylosoxidans, an opportunistic pathogen and a denitrifying bacterium of importance in the nitrogen cycle. This high-resolution structure provides insight into electron, substrate, and proton pathways, and provides evidence that the quinol binding site not only contains the conserved His and Asp residues but also possesses a critical Arg (Arg720) observed in cytochrome bo<sub>3</sub>, a respiratory quinol oxidase.

Item Type:	Article
Uncontrolled Keywords:	Bacteria, Nitric Oxide, Hydroquinones, Oxidoreductases
Divisions:	Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology
Depositing User:	Symplectic Admin
Date Deposited:	06 Jul 2023 15:52
Last Modified:	21 Oct 2023 08:22
DOI:	10.1038/s41467-023-39140-x
Open Access URL:	https://europepmc.org/backend/ptpmcrender.fcgi?acc...
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3171514