8bgw

Publication Abstract from PubMed

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 A 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(3), a respiratory quinol oxidase.

A 2.2 A cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases.,Flynn AJ, Antonyuk SV, Eady RR, Muench SP, Hasnain SS Nat Commun. 2023 Jun 9;14(1):3416. doi: 10.1038/s41467-023-39140-x. PMID:37296134^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.