Foote N, Peterson J, Gadsby P M, Greenwood C, Thomson A J
Biochem J. 1984 Oct 15;223(2):369-78. doi: 10.1042/bj2230369.
The magnetic properties at different temperatures of oxidized Pseudomonas aeruginosa cytochrome c-551 peroxidase were studied, with the use of the technique of magnetic-circular-dichroism spectroscopy. At 4.2K, both constituent haems were found to be low-spin, and the axial ligand pairs were identified as histidine-histidine and histidine-methionine. At room temperature high-spin signals were observed, amounting to less than 25% of the total haem present. These signals are concluded to arise mainly from a temperature-dependent spin-state equilibrium in the methionine-ligated haem.
利用磁圆二色光谱技术研究了氧化型铜绿假单胞菌细胞色素c-551过氧化物酶在不同温度下的磁性特性。在4.2K时,发现两个组成血红素均为低自旋态,且轴向配体对被确定为组氨酸-组氨酸和组氨酸-甲硫氨酸。在室温下观察到高自旋信号,其占总血红素的比例不到25%。得出这些信号主要源于甲硫氨酸连接的血红素中温度依赖性的自旋态平衡。