A cytochrome c oxidase model catalyzes oxygen to water reduction under rate-limiting electron flux
A cytochrome c oxidase model catalyzes oxygen to water reduction under rate-limiting electron flux
复制标题
DOI：
10.1126/science.1135844
复制
发表时间：
2007-03-16
期刊：
影响因子：
56.9
通讯作者：
Chidsey, Christopher E. D.
中科院分区：
文献类型：
--
作者：
Collman, James P.;Devaraj, Neal K.;Chidsey, Christopher E. D.
我们研究了细胞色素c氧化酶活性位点的功能模型的选择性，该功能模型模拟了Fe-a3、Cu-B和Tyr（244）的配位环境和相对位置。为了控制电子通量，我们将该模型和缺乏铜和苯酚的类似物共价连接到自组装单层涂覆的金电极上。当电子转移速率被限制时，铜和苯酚都需要增强氧向水的选择性还原。这一发现支持的假设，在稳态营业额，这些氧化还原中心的主要作用是迅速提供所需的所有电子，以减少氧气的四个电子，从而防止释放有毒的部分还原氧物种。
We studied the selectivity of a functional model of cytochrome c oxidase's active site that mimics the coordination environment and relative locations of Fe-a3, Cu-B, and Tyr(244). To control electron flux, we covalently attached this model and analogs lacking copper and phenol onto self-assembled monolayer-coated gold electrodes. When the electron transfer rate was made rate limiting, both copper and phenol were required to enhance selective reduction of oxygen to water. This finding supports the hypothesis that, during steady-state turnover, the primary role of these redox centers is to rapidly provide all the electrons needed to reduce oxygen by four electrons, thus preventing the release of toxic partially reduced oxygen species.