反硝化副球菌双亚基细胞色素aa3的电位和光谱研究。与13亚基牛心酶的比较。
Potentiometric and spectral studies with the two-subunit cytochrome aa3 from Paracoccus denitrificans. Comparison with the 13-subunit beef heart enzyme.
作者信息
Pardhasaradhi K, Ludwig B, Hendler R W
机构信息
Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.
出版信息
Biophys J. 1991 Aug;60(2):408-14. doi: 10.1016/S0006-3495(91)82066-5.
Abstract
Previous work from this laboratory has revealed a complex and interactive redox behavior for the active metal centers in beef heart cytochrome aa3. All of these centers are contained in two of the 13 subunits which make up the enzyme. The isolated cytochrome aa3 of Paracoccus denitrificans contains only two subunits. The purpose of the current investigation was to see if the complex redox behavior is dependent on the presence of the additional 11 peptides that are present in the mammalian enzyme. In this paper we report that the structurally simpler bacterial enzyme displays a redox behavior which is very similar to that seen with the mammalian enzyme. Therefore, the observed redox behavior does not depend on interactions involving the additional peptides.
摘要
该实验室之前的研究揭示了牛心细胞色素aa3中活性金属中心复杂的相互作用的氧化还原行为。所有这些中心都包含在构成该酶的13个亚基中的两个亚基中。反硝化副球菌分离出的细胞色素aa3仅包含两个亚基。当前研究的目的是探究这种复杂的氧化还原行为是否依赖于哺乳动物酶中存在的另外11种肽段。在本文中，我们报告结构更简单的细菌酶表现出与哺乳动物酶非常相似的氧化还原行为。因此，观察到的氧化还原行为并不依赖于涉及其他肽段的相互作用。
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