Fee J A, Yoshida T, Surerus K K, Mather M W
Division of Isotope and Nuclear Chemistry, Los Alamos National Laboratory, New Mexico 87545.
J Bioenerg Biomembr. 1993 Apr;25(2):103-14. doi: 10.1007/BF00762852.
The subject of this short review is the cytochrome c oxidase (caa3) from the thermophilic bacterium Thermus thermophilus. First, some of the extensive physical and enzymological results obtained with this enzyme are reviewed, and two experiments are described, involving isotope substitutions in combination with Mössbauer and ENDOR spectroscopies, which have provided novel insight into the active sites of the enzyme. Second, we summarize recent molecular genetic work showing that Thermus cytochrome caa3 is a bona fide member of the superfamily of heme-copper oxidases. Finally, we present a rough three-dimensional model and speculate about certain features of the metal-binding sites.
本简短综述的主题是嗜热栖热菌中的细胞色素c氧化酶（caa3）。首先，回顾了用该酶获得的一些广泛的物理和酶学研究结果，并描述了两个实验，这些实验涉及同位素取代与穆斯堡尔光谱和电子核双共振光谱相结合，为该酶的活性位点提供了新的见解。其次，我们总结了最近的分子遗传学研究工作，表明栖热菌细胞色素caa3是血红素-铜氧化酶超家族的一个真正成员。最后，我们提出了一个大致的三维模型，并推测了金属结合位点的某些特征。
