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Title | A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases. |
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Journal, issue, pages | Nat Commun, Vol. 14, Issue 1, Page 3416, Year 2023 |
Publish date | Jun 9, 2023 |
![]() | Alex J Flynn / Svetlana V Antonyuk / Robert R Eady / Stephen P Muench / S Samar Hasnain / ![]() |
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 ...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. |
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Methods | EM (single particle) |
Resolution | 2.2 Å |
Structure data | EMDB-16041, PDB-8bgw: |
Chemicals | ![]() ChemComp-HEM: ![]() ChemComp-FE: ![]() ChemComp-CA: ![]() ChemComp-10M: ![]() ChemComp-UQ1: ![]() ChemComp-LOP: ![]() ChemComp-HOH: |
Source |
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![]() | MEMBRANE PROTEIN / quinol-dependent Nitric Oxide Reductase / proton transfer / quinol binding / ubiquinol oxidase |