Journal
SCIENCE ADVANCES
Volume 5, Issue 8, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.aax1803
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Funding
- BBSRC [BB/L006960/1, BB/N013972/1]
- RIKEN-Liverpool International Programme Associate studentship
- SFTC's ASTEC department
- Wellcome Trust [109158/B/15/Z, 108466/Z/15/Z]
- BBSRC [BB/N013972/1, BB/L006960/1, BB/S020055/1] Funding Source: UKRI
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Quinol-dependent nitric oxide reductases (qNORs) are membrane-integrated, iron-containing enzymes of the denitrification pathway, which catalyze the reduction of nitric oxide (NO) to the major ozone destroying gas nitrous oxide (N2O). Cryo-electron microscopy structures of active qNOR from Alcaligenes xylosoxidans and an activity-enhancing mutant have been determined to be at local resolutions of 3.7 and 3.2 angstrom, respectively. They unexpectedly reveal a dimeric conformation (also confirmed for qNOR from Neisseria meningitidis) and define the active-site configuration, with a clear water channel from the cytoplasm. Structure-based mutagenesis has identified key residues involved in proton transport and substrate delivery to the active site of qNORs. The proton supply direction differs from cytochrome c-dependent NOR (cNOR), where water molecules from the cytoplasm serve as a proton source similar to those from cytochrome c oxidase.
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