Crystallographic Studies of the Biuret Reaction
Crystallographic Studies of the Biuret Reaction
复制标题
缩二脲反应的晶体学研究
DOI：
10.1038/184707a0
复制
发表时间：
1959
期刊：
影响因子：
64.8
通讯作者：
J. C. Taylor
中科院分区：
文献类型：
--
作者：
H. C. Freeman;J. E. Smith;J. C. Taylor
金属离子和多肽之间的HE键是一个日益引起生物化学兴趣的课题。金属肽复合物似乎参与了金属活化的蛋白水解酶反应的过渡状态*，铜离子抑制明胶的凝胶化（参考文献3和Kiefer， M., and Vinograd, JR ., private communication），以及金属蛋白溶液颜色的形成***。迄今为止，这类配合物结构的证据是从溶液中提取的，因为它们与已经研究过的少数氨基酸螯合物的晶体结构之间没有足够的相似性****。因此，我们已经开始确定几种化合物的结构，以作为肽-金属相互作用的模型。在本通讯中，我们希望报告其中两个结构的特征，这些特征似乎具有生物化学意义。
HE bonding between metal ions and peptides is a subject of increasing biochemical interest. Metal-peptide complexes appear to be involved inter alia in the transition-states of metal-activated proteo-lytic enzyme reactions*, in the inhibition of the gelation of gelatine by cupric ions (ref. 3 and Kiefer, M., and Vinograd, JR, private communication), and in the formation of the colours of metal-protein solutions***. Hitherto, the evidence for the struc-tures of such complexes has been drawn from moasuro-ments on solutions, since insufficient analogy exists between them and the few amino-acid chelates the crystal structures of which have been studied****. We have therefore begun structure determinations of several compounds intended to be models for peptide-metal interaction. In this communication we wish to report those features of two of these structures which appear to be of biochemical significance.