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

TY - JOUR

T1 - Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus

AU - Matsumoto, Yushi

AU - Tosha, Takehito

AU - Pisliakov, Andrei V.

AU - Hino, Tomoya

AU - Sugimoto, Hiroshi

AU - Nagano, Shingo

AU - Sugita, Yuji

AU - Shiro, Yoshitsugu

PY - 2012/2

Y1 - 2012/2

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/84856734126

U2 - 10.1038/nsmb.2213

DO - 10.1038/nsmb.2213

M3 - Article

C2 - 22266822

AN - SCOPUS:84856734126

SN - 1545-9993

VL - 19

SP - 238

EP - 245

JO - Nature Structural & Molecular Biology

JF - Nature Structural & Molecular Biology

IS - 2

ER -