Hunter D J, Moody A J, Rich P R, Ingledew W J
School of Biological and Medical Sciences, University of St. Andrews, Fife, Scotland, UK.
FEBS Lett. 1997 Jul 21;412(1):43-7. doi: 10.1016/s0014-5793(97)00735-7.
The spectroscopic and ligand-binding properties of a copper-deficient cytochrome bo3, a member of the haem-copper superfamily of terminal oxidases, are reported and contrasted with those of the native enzyme. The enzyme lacks the copper atom (CuB) which is normally an integral part of the catalytic site. The consequences of loss of the CuB are the loss of antiferromagnetic coupling to the high-spin haem and an inability to form any of the integer-spin derivatives of the enzyme. Low-spin compounds of the normally high-spin haem are still formed with appropriate ligands, although these are modified.
本文报道了一种缺乏铜的细胞色素bo3（末端氧化酶血红素-铜超家族的成员）的光谱和配体结合特性，并将其与天然酶的特性进行了对比。该酶缺少通常作为催化位点不可或缺一部分的铜原子（CuB）。CuB缺失的后果是失去与高自旋血红素的反铁磁耦合，并且无法形成该酶的任何整数自旋衍生物。尽管会发生修饰，但通常的高自旋血红素的低自旋化合物仍会与适当的配体形成。
