来自硝酸还原硫碱弧菌的细胞色素c亚硝酸还原酶的结晶及初步X射线分析。
Crystallization and preliminary X-ray analysis of cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens.
作者信息
Boyko K M, Polyakov K M, Tikhonova T V, Slutsky A, Antipov A N, Zvyagilskaya R A, Bourenkov G P, Popov A N, Lamzin V S, Popov V O
机构信息
A. N. Bakh Institute of Biochemistry, RAS, Moscow, Russia.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt 3):215-7. doi: 10.1107/S174430910600296X. Epub 2006 Feb 10.
A novel cytochrome c nitrite reductase (TvNiR) was isolated from the haloalkalophilic bacterium Thioalkalivibrio nitratireducens. The enzyme catalyses nitrite and hydroxylamine reduction, with ammonia as the only product of both reactions. It consists of 525 amino-acid residues and contains eight haems c. TvNiR crystals were grown by the hanging-drop vapour-diffusion technique. The crystals display cubic symmetry and belong to space group P2(1)3, with unit-cell parameter a = 194 A. A native data set was obtained to 1.5 A resolution. The structure was solved by the SAD technique using the data collected at the Fe absorption peak wavelength.
从嗜盐碱细菌嗜碱硝酸还原硫杆菌中分离出一种新型细胞色素c亚硝酸还原酶（TvNiR）。该酶催化亚硝酸盐和羟胺还原反应，两个反应的唯一产物均为氨。它由525个氨基酸残基组成，含有8个c型血红素。通过悬滴气相扩散技术培养了TvNiR晶体。这些晶体呈立方对称，属于空间群P2(1)3，晶胞参数a = 194 Å。获得了分辨率为1.5 Å的天然数据集。利用在铁吸收峰波长处收集的数据，通过单波长反常散射（SAD）技术解析了其结构。
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