8BGW

CryoEM structure of quinol-dependent Nitric Oxide Reductase (qNOR) from Alcaligenes xylosoxidans at 2.2 A resolution

Summary for 8BGW

• Entry DOI: 10.2210/pdb8bgw/pdb
• EMDB information: 16041
• Descriptor: Nitric oxide reductase subunit B, PROTOPORPHYRIN IX CONTAINING FE, FE (III) ION, ... (8 entities in total)
• Functional Keywords: quinol-dependent nitric oxide reductase, proton transfer, quinol binding, ubiquinol oxidase, membrane protein
• Biological source: Achromobacter xylosoxidans
• Total number of polymer chains: 2
• Total formula weight: 182209.93

Authors

Flynn, A.,Antonyuk, S.V.,Eady, R.R.,Muench, S.P.,Hasnain, S.S. (deposition date: 2022-10-28, release date: 2023-08-16)

Primary citation

Flynn, A.J.,Antonyuk, S.V.,Eady, R.R.,Muench, S.P.,Hasnain, S.S.
A 2.2 angstrom cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases.
Nat Commun, 14:3416-3416, 2023

PubMed 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, a respiratory quinol oxidase.

PubMed: 37296134
DOI: 10.1038/s41467-023-39140-x

Experimental method

ELECTRON MICROSCOPY (2.2 Å)