Jan 24, 2012

Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus

Nature Structural & Molecular Biology
Yushi MatsumotoYoshitsugu Shiro


The structure of quinol-dependent nitric oxide reductase (qNOR) from G. stearothermophilus, which catalyzes the reduction of NO to produce the major ozone-depleting gas N(2)O, has been characterized at 2.5 Å resolution. The overall fold of qNOR is similar to that of cytochrome c-dependent NOR (cNOR), and some structural features that are characteristic of cNOR, such as the calcium binding site and hydrophilic cytochrome c domain, are observed in qNOR, even though it harbors no heme c. In contrast to cNOR, structure-based mutagenesis and molecular dynamics simulation studies of qNOR suggest that a water channel from the cytoplasm can serve as a proton transfer pathway for the catalytic reaction. Further structural comparison of qNOR with cNOR and aerobic and microaerobic respiratory oxidases elucidates their evolutionary relationship and possible functional conversions.

  • References55
  • Citations42


Mentioned in this Paper

Molecular Dynamics
Biochemical Pathway
Nitric oxide reductase
NorZ protein, Alcaligenes eutrophus
Mutagenesis, Site-Directed
Mutant Proteins
Crystallography, X-Ray
Water channel
Protein Conformation

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