Banci L, Bertini I, Luchinat C, Scozzafava A
Department of Chemistry, University of Florence, Italy.
J Biol Chem. 1989 Jun 15;264(17):9742-4.
The 1H NMR spectra of the cyanide adduct of Cu2Co2-superoxide dismutase have been remeasured at pH 7.5. The exchange rate of CN- is slow on the NMR time scale. The correlation with the spectrum of the unligated enzyme has been established through saturation-transfer techniques of the system in which 50% of the cyanide adduct is formed and through comparison with the spectrum of a Cu2Co2-superoxide dismutase-CN- sample in which the histidines have been deuterium labeled at the position epsilon 1. The similarities between the spectra of the CN- and N-3 derivatives are stressed, in particular with respect to the removal from copper coordination of the same histidine, assigned as His-46.
已在pH 7.5条件下重新测量了Cu2Co2 - 超氧化物歧化酶氰化物加合物的1H NMR谱。在NMR时间尺度上，CN-的交换速率较慢。通过在形成50%氰化物加合物的系统中采用饱和转移技术，并与组氨酸在ε1位置进行了氘代标记的Cu2Co2 - 超氧化物歧化酶 - CN-样品的谱图进行比较，建立了与未结合配体的酶谱的相关性。强调了CN-和N-3衍生物谱图之间的相似性，特别是在从铜配位中去除同一组氨酸（指定为His - 46）方面。
