细胞色素氧化酶模型。
A model for cytochrome oxidase.
作者信息
Palmer G, Babcock G T, Vickery L E
出版信息
Proc Natl Acad Sci U S A. 1976 Jul;73(7):2206-10. doi: 10.1073/pnas.73.7.2206.
Abstract
A model is proposed for the active center of cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) in which cytochrome a is a low-spin ferrihemoprotein and cytochrome a3 is a high-spin ferrihemoprotein antiferromagnetically coupled to one of the two Cu2+ ions present in the enzyme. It is further proposed that reduction is accompanied by a conformational change in the enzyme thus exposing the sixth coordination site of cytochrome a3 to ligands. With this model it is possible to account for a variety of outstanding observations including the results of magnetic circular dichroism, Mossbauer, and electron paramagnetic resonance spectroscopies, as well as magnetic susceptibility measurements.
摘要
提出了一种细胞色素c氧化酶（亚铁细胞色素c：氧氧化还原酶，EC 1.9.3.1）活性中心的模型，其中细胞色素a是低自旋高铁血红蛋白，细胞色素a3是高自旋高铁血红蛋白，与酶中存在的两个Cu2+离子之一反铁磁耦合。进一步提出，还原过程伴随着酶的构象变化，从而使细胞色素a3的第六个配位位点暴露于配体。基于该模型，可以解释各种突出的观察结果，包括磁圆二色性、穆斯堡尔和电子顺磁共振光谱的结果，以及磁化率测量结果。
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