Maret W, Kozłowski H
Biochim Biophys Acta. 1987 Apr 30;912(3):329-37. doi: 10.1016/0167-4838(87)90036-7.
Blue and non-blue states of the copper center in copper-substituted alcohol dehydrogenase (EC 1.1.1.1) can be attained by coenzyme binding and/or ligand binding to the copper ion. Copper alcohol dehydrogenase has been studied by electronic absorption, CD and EPR spectroscopy in the presence and absence of coenzyme. On the basis of previous work on blue (Type 1) copper proteins with a CuSS*N2 chromophore the assignment of charge transfer transitions in copper alcohol dehydrogenase is discussed. The latter contains a CuS2N(OH2) unit in the ligand-free protein and a CuS2N2 unit in the ternary complex with NAD+ and pyrazole. It is proposed that the energy of the charge transfer transitions can be used as a structural marker in combination with EPR data. A comparison is made between the spectroscopic properties of the ternary complex of copper alcohol dehydrogenase and the copper centers in stellacyanin and cytochrome-c oxidase (CuA) in order to test the validity of recent structural models of the type CuS2N2, i.e., a cupric ion coordinated to two thiolate ligands. Finally, a close resemblance between the electronic absorption spectra of copper alcohol dehydrogenase and those of other variants of Type 1 copper centers such as the 'unusual' copper center of nitrous oxide reductase is noted as an indication of similar coordination environments.
铜取代乙醇脱氢酶（EC 1.1.1.1）中铜中心的蓝色和非蓝色状态可通过辅酶结合和/或配体与铜离子的结合来实现。在有和没有辅酶的情况下，已通过电子吸收、圆二色光谱（CD）和电子顺磁共振光谱（EPR）对铜乙醇脱氢酶进行了研究。基于先前对具有CuSS*N2发色团的蓝色（1型）铜蛋白的研究，讨论了铜乙醇脱氢酶中电荷转移跃迁的归属。在无配体的蛋白质中，后者含有一个CuS2N(OH2)单元，在与NAD+和吡唑形成的三元复合物中含有一个CuS2N2单元。有人提出，电荷转移跃迁的能量可与EPR数据结合用作结构标记。对铜乙醇脱氢酶的三元复合物与星蓝蛋白和细胞色素c氧化酶（CuA）中的铜中心的光谱性质进行了比较，以检验最近的CuS2N2类型结构模型的有效性，即一个铜离子与两个硫醇盐配体配位。最后，注意到铜乙醇脱氢酶的电子吸收光谱与1型铜中心的其他变体（如一氧化二氮还原酶的“异常”铜中心）的电子吸收光谱非常相似，这表明它们具有相似的配位环境。
