Connelly P R, Johnson C R, Robert C H, Bak H J, Gill S J
Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.
J Mol Biol. 1989 Jun 20;207(4):829-32. doi: 10.1016/0022-2836(89)90248-9.
A high precision, two-dimensional study of oxygen and carbon monoxide binding to Panulirus interruptus hemocyanin has been carried out. Global data analysis of three types of experiments, probing the molecule in its various states of CO and O2 ligation, revealed the entire hexamer to be the basic allosteric unit involved in a two-state mechanism. The co-operativity and linkage of the two ligands are presented in terms of derivative Hill plot surfaces extended along co-ordinates of CO and O2 activities giving a detailed and comprehensive view of the binding behavior. Among the findings is an apparent high co-operativity of carbon monoxide binding at high oxygen activity. The results are discussed in view of a general mechanism for co-operative behavior found in larger hemocyanin aggregates concerning "nested" allosteric interactions.
对中断沟龙虾血蓝蛋白与氧气和一氧化碳结合进行了高精度的二维研究。对三种类型的实验进行全局数据分析，这些实验探测了该分子在一氧化碳和氧气结合的各种状态下的情况，结果表明整个六聚体是参与双态机制的基本别构单元。两种配体的协同性和关联性通过沿一氧化碳和氧气活性坐标扩展的导数希尔图表面来呈现，从而对结合行为给出详细而全面的视图。研究结果之一是在高氧活性下一氧化碳结合表现出明显的高协同性。鉴于在较大的血蓝蛋白聚集体中发现的关于“嵌套”别构相互作用的协同行为一般机制，对这些结果进行了讨论。
