CONFORMATION, CO-OPERATIVITY AND LIGAND-BINDING IN HUMAN HEMOGLOBIN
CONFORMATION, CO-OPERATIVITY AND LIGAND-BINDING IN HUMAN HEMOGLOBIN
复制标题
DOI:
10.1016/0022-2836(75)90382-4
复制
发表时间:
1975-01-01
影响因子:
5.6
通讯作者:
GIBSON, QH
中科院分区:
文献类型:
--
作者:
CASSOLY, R;GIBSON, QH
There does not appear to be any co-operativity manifest in the four combination rate constants for the binding of nitric oxide to deoxyhemoglobin. The time-course of the observed reaction is best fitted by statistically related rates, and the numerical relation between the rate constants for the binding of the fourth molecule of carbon monoxide and the fourth molecule of nitric oxide, which can be obtained independently, also argues for a statistical relation between the nitric oxide binding rate constants.In spite of the absence of co-operativity, the normal T → R transition occurs on nitric oxide binding, as demonstrated by the release of 8-hydroxy-1,3,6-pyrene trisulfonate, and the R-state shows the normal enhancement of reactivity towards carbon monoxide as compared with the T-state (30-fold).Competition experiments between carbon monoxide and nitric oxide in which the two ligands react simultaneously with deoxyhemoglobin suggest that the switching point (T → R) occurs on the average after 2.7 molecules of nitric oxide have been bound (in 0.05m-2,2-bis(hydroxymethyl)-2,2′,2″-nitrilotriethanol, pH 7) and after 3 molecules of carbon monoxide (in 0.05m-phosphate, PH 7).