A STUDY OF THE OXIDIZED FORM OF PSEUDOMONAS-AERUGINOSA CYTOCHROME-C-551 PEROXIDASE WITH THE USE OF MAGNETIC CIRCULAR-DICHROISM
A STUDY OF THE OXIDIZED FORM OF PSEUDOMONAS-AERUGINOSA CYTOCHROME-C-551 PEROXIDASE WITH THE USE OF MAGNETIC CIRCULAR-DICHROISM
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DOI：
10.1042/bj2230369
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发表时间：
1984-01-01
影响因子：
4.1
通讯作者：
THOMSON, AJ
中科院分区：
文献类型：
--
作者：
FOOTE, N;PETERSON, J;THOMSON, AJ
利用磁圆二色光谱技术研究了氧化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特性。 4.2 度。 K，两种组成血红素都是低自旋的，轴向配体对被鉴定为组氨酸-组氨酸和组氨酸-蛋氨酸。在室温下观察到高自旋信号，其含量小于总血红素的 25%。这些信号被推断主要来自于蛋氨酸连接的血红素中依赖于温度的自旋态平衡。
The magnetic properties at different temperatures of oxidized P. aeruginosa cytochrome c-551 peroxidase were studied, with the use of the technique of magnetic-circular-dichroism spectroscopy. At 4.2.degree. K, both constituent hemes were 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 < 25% of the total heme present. These signals are concluded to arise mainly from a temperature-dependent spin-state equilibrium in the methionine-ligated heme.