Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme

Scientific Reports
Nathalie GonskaPia Adelroth

Abstract

Bacterial nitric oxide reductases (NORs) catalyse the reduction of NO to N2O and H2O. NORs are found either in denitrification chains, or in pathogens where their primary role is detoxification of NO produced by the immune defense of the host. Although NORs belong to the heme-copper oxidase superfamily, comprising proton-pumping O2-reducing enzymes, the best studied NORs, cNORs (cytochrome c-dependent), are non-electrogenic. Here, we focus on another type of NOR, qNOR (quinol-dependent). Recombinant qNOR from Neisseria meningitidis, a human pathogen, purified from Escherichia coli, showed high catalytic activity and spectroscopic properties largely similar to cNORs. However, in contrast to cNOR, liposome-reconstituted qNOR showed respiratory control ratios above two, indicating that NO reduction by qNOR was electrogenic. Further, we determined a 4.5 Å crystal structure of the N. meningitidis qNOR, allowing exploration of a potential proton transfer pathway from the cytoplasm by mutagenesis. Most mutations had little effect on the activity, however the E-498 variants were largely inactive, while the corresponding substitution in cNOR was previously shown not to induce significant effects. We thus suggest that, contrary to cNOR, ...Continue Reading

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Citations

Jul 3, 2020·Environmental Microbiology Reports·Nadia SzeinbaumJennifer B Glass
Jan 14, 2021·Nature Reviews. Microbiology·Ville R I Kaila, Mårten Wikström
Jan 6, 2021·Chemical Reviews·Filipa CalistoManuela M Pereira
Feb 29, 2020·Chemical Reviews·Christina FerousiKyle M Lancaster
Aug 28, 2021·Microorganisms·Jose María Miralles-RobledilloCarmen Pire

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Methods Mentioned

BETA
X-ray
PCR
gel-filtration

Software Mentioned

PHENIX suite
AutoPROC
Gs
COOT
Phaser
Aimless
Nm
REFMAC

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