Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus
Copyright policy )Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus
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.
- University of Dundee United Kingdom
- Tottori University Japan
- RIKEN Advanced Science Institute Japan
- RIKEN Japan
Models, Molecular, Protein Conformation, Nitrous Oxide, 500, Molecular Dynamics Simulation, Crystallography, X-Ray, Nitric Oxide, 530, Hydroquinones, Geobacillus stearothermophilus, Amino Acid Substitution, Mutagenesis, Site-Directed, Mutant Proteins, Oxidoreductases
Models, Molecular, Protein Conformation, Nitrous Oxide, 500, Molecular Dynamics Simulation, Crystallography, X-Ray, Nitric Oxide, 530, Hydroquinones, Geobacillus stearothermophilus, Amino Acid Substitution, Mutagenesis, Site-Directed, Mutant Proteins, Oxidoreductases
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