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首页> 外文期刊>Nature structural biology >CRYSTAL STRUCTURE OF NITRIC OXIDE REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM
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CRYSTAL STRUCTURE OF NITRIC OXIDE REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM

机译:镰刀菌镰刀菌脱硝一氧化氮还原酶的晶体结构

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Structures of nitric oxide reductase (NOR) in the ferric resting and the ferrous CO states have been solved at 2.0 Angstrom resolution. These structures provide significant new insights into how NO is reduced in biological systems, The haem distal pocket is open to solvent, implicating this region as a possible NADH binding site, In combination with mutagenesis results, a hydrogen-bonding network from the water molecule adjacent to the iron ligand to the protein surface of the distal pocket through the hydroxyl group of Ser 286 and the carboxyl group of Asp 393 can be assigned to a pathway for proton delivery during the NO reduction reaction. [References: 42]
机译:一氧化氮还原酶(NOR)的结构在铁静止和亚铁一氧化碳状态已解决在2.0埃分辨率。这些结构为生物系统中NO的还原提供了重要的新见识。血红素远端囊对溶剂开放,暗示该区域可能是NADH结合位点。与诱变作用相结合,邻近水分子的氢键网络通过Ser 286的羟基和Asp 393的羧基将铁配体与远端口袋的蛋白质表面结合,可以分配给NO还原反应过程中质子传递的途径。 [参考:42]

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