Foote N, Peterson J, Gadsby P M, Greenwood C, Thomson A J
Biochem J. 1985 Aug 15;230(1):227-37. doi: 10.1042/bj2300227.
Magnetic-c.d., e.p.r. and optical-absorption spectra are reported for the half-reduced form of Pseudomonas aeruginosa cytochrome c-551 peroxidase, a di-haem protein, and its fluoride derivative. Comparison of this enzyme species with oxidized peroxidase shows the occurrence of spin-state changes at both haem sites. The high-potential haem changes its state from partially high-spin to low-spin upon reduction. This is linked to a structural alteration at the ferric low-potential haem group, causing it to change from low-spin to high-spin. Low-temperature spectra demonstrate photolysis of an endogenous ligand of the high-potential haem. In addition, an inactive form of enzyme is examined in which the structural change at the ferric low-potential haem does not occur on reduction of the high-potential haem.
报道了铜绿假单胞菌细胞色素c-551过氧化物酶(一种双血红素蛋白)及其氟化物衍生物的半还原形式的磁圆二色性(Magnetic-c.d.)、电子顺磁共振(e.p.r.)和光吸收光谱。将这种酶与氧化过氧化物酶进行比较,发现在两个血红素位点都发生了自旋态变化。高电位血红素在还原时从部分高自旋态转变为低自旋态。这与三价铁低电位血红素基团的结构改变有关,导致其从低自旋态转变为高自旋态。低温光谱显示高电位血红素的内源性配体发生了光解。此外,还研究了一种无活性形式的酶,其中在高电位血红素还原时,三价铁低电位血红素没有发生结构变化。