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

Yushi Matsumoto, Takehito Tosha, Andrei V. Pisliakov, Tomoya Hino, Hiroshi Sugimoto, Shingo Nagano (Lead / Corresponding author), Yuji Sugita, Yoshitsugu Shiro (Lead / Corresponding author)

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    96 Citations (Scopus)


    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 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.
    Original languageEnglish
    Pages (from-to)238-245
    Number of pages8
    JournalNature Structural & Molecular Biology
    Issue number2
    Publication statusPublished - Feb 2012


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