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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/B3Y963_GEOSE B3Y963_GEOSE] | | [https://www.uniprot.org/uniprot/B3Y963_GEOSE B3Y963_GEOSE] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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 A 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.
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| Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus.,Matsumoto Y, Tosha T, Pisliakov AV, Hino T, Sugimoto H, Nagano S, Sugita Y, Shiro Y Nat Struct Mol Biol. 2012 Jan 22;19(2):238-45. doi: 10.1038/nsmb.2213. PMID:22266822<ref>PMID:22266822</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3ayf" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]] | | *[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |