绿球藻硝酸还原酶的部分纯化、细胞色素含量及体内失活后氰化氢的存在。
Nitrate reductase of Chlorella fusca: Partial purification, cytochrome content and presence of HCN after in vivo inactivation.
机构信息
Forschungsstelle Vennesland der Max-Planck-Gesellschaft, Harnackstraße 23, D-1000, Berlin 33.
出版信息
Planta. 1978 Jan;141(3):323-8. doi: 10.1007/BF00388351.
An inactivated nitrate reductase (EC 1.6.6.1) formed in vivo by the green alga Chlorella fusca Shihira and Kraus is shown to be a cyanide complex. The partially purified inactive enzyme releases 0.048 nmol of HCN per unit of enzyme activated. This compares with 0.066 nmol of HCN liberated in similar previous measurements with the inactivated enzyme from Chlorella vulgaris. The nitrate reductase from C. fusca has been purified to a level of 67 μmol nitrate reduced per min per mg enzyme. It contains a cytochrome b557, at a level 1.9-fold higher per unit of active enzyme, than the nitrate reductase from C. vulgaris.
由绿藻 Chlorella fusca Shihira 和 Kraus 体内形成的一种失活的硝酸盐还原酶（EC 1.6.6.1）被证明是一种氰化物络合物。部分纯化的无活性酶每单位酶激活后释放 0.048 nmol 的 HCN。这与以前用来自普通小球藻的失活酶进行的类似测量中释放的 0.066 nmol HCN 相比。来自 C. fusca 的硝酸盐还原酶已被纯化至每毫克酶每分钟还原 67 μmol 硝酸盐的水平。它含有细胞色素 b557，其活性酶单位的含量比来自普通小球藻的硝酸盐还原酶高 1.9 倍。
Zotero 插件