Raphael A L, Gray H B
Arthur Amos Noyes Laboratory, California Institute of Technology, Pasadena 91125.
Proteins. 1989;6(3):338-40. doi: 10.1002/prot.340060316.
Semisynthesis has been employed to replace the axial methionine in horse heart cytochrome c with histidine. The reduction potential of the His-80 protein (cyt c-His-80) is 41 mV vs NHE (0.1 M phosphate; pH 7.0; 25 degrees C). The absorption spectra of oxidized and reduced cyt c-His-80 are very similar to those of the native protein in the porphyrin region, but the 695 nm band is absent in the oxidized His-80 protein.
已采用半合成法将马心细胞色素c中的轴向甲硫氨酸替换为组氨酸。His-80蛋白(细胞色素c-His-80)相对于标准氢电极(NHE,0.1M磷酸盐;pH 7.0;25℃)的还原电位为41mV。氧化型和还原型细胞色素c-His-80在卟啉区域的吸收光谱与天然蛋白的吸收光谱非常相似,但氧化型His-80蛋白中不存在695nm的吸收带。