Einsle Oliver, Stach Petra, Messerschmidt Albrecht, Klimmek Oliver, Simon Jörg, Kröger Achim, Kroneck Peter M H
Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, 82152 Martinsried, Germany.
Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):341-2. doi: 10.1107/s090744490102039x. Epub 2002 Jan 24.
Crystals of the complex between the enzyme cytochrome c nitrite reductase (NrfA) and the membrane-bound quinol oxidase and electron carrier NrfH were grown by vapour diffusion using ammonium sulfate as a precipitant. In the epsilon-proteobacterium Wolinella succinogenes, NrfA and NrfH form a functional membrane-bound complex which catalyzes the last step in the metabolic pathway of nitrate dissimilation. NrfH represents a prototype of a large family of putative bacterial quinol oxidases, the NapC/NirT family, which have been proposed to serve as electron donors for a variety of reductases. Crystal growth of the NrfHA complex was strongly dependent on the presence of detergent; the crystals grown belonged to space group I422.
通过以硫酸铵作为沉淀剂的气相扩散法,培养了细胞色素c亚硝酸还原酶(NrfA)与膜结合喹啉氧化酶及电子载体NrfH之间复合物的晶体。在ε-变形菌沃氏琥珀酸弧菌中,NrfA和NrfH形成一种功能性的膜结合复合物,该复合物催化硝酸盐异化代谢途径中的最后一步。NrfH代表一大类假定的细菌喹啉氧化酶(NapC/NirT家族)的一个原型,有人提出这些酶可作为多种还原酶的电子供体。NrfHA复合物的晶体生长强烈依赖于去污剂的存在;所生长的晶体属于空间群I422。