Spectroscopic and computational insights into the geometric and electronic properties of the A-cluster of acetyl-coenzyme A synthase
Spectroscopic and computational insights into the geometric and electronic properties of the A-cluster of acetyl-coenzyme A synthase
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DOI：
10.1007/s00775-004-0566-8
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发表时间：
2004-07-01
影响因子：
3
通讯作者：
Brunold, TC
中科院分区：
文献类型：
--
作者：
Brunold, TC
在过去的二十年中，双功能酶乙酰辅酶A合酶/一氧化碳脱氢酶（ACS/CODH）从Moorella热醋酸一直是相当多的研究的主题，旨在阐明的几何和电子性质的A-簇，作为ACS催化的活性位点。虽然最近在获得这种酶的高分辨率X射线结构方面的成功解决了许多关于A簇金属中心的数量、身份和配位环境的谜团，但关于这种高度复杂的多核活性位点的催化机制的基本问题尚未得到回答。这篇评论总结了从光谱和计算研究中获得的关于A-团簇的氧化、还原和CO结合形式的相关信息，并强调了在未来研究中需要解决的关于该团簇的电子性质和反应性的一些关键问题。
For the last two decades, the bifunctional enzyme acetyl-coenzyme A synthase/carbon monoxide dehydrogenase (ACS/CODH) from Moorella thermoacetica has been the subject of considerable research aimed at elucidating the geometric and electronic properties of the A-cluster, which serves as the active site for ACS catalysis. While the recent success in obtaining high-resolution X-ray structures of this enzyme solved many of the mysteries regarding the number, identities, and coordination environments of the metal centers of the A-cluster, fundamental questions concerning the catalytic mechanism of this highly elaborate polynuclear active site have yet to be answered. This Commentary summarizes relevant information obtained from spectroscopic and computational studies on the oxidized, reduced, and CO-bound forms of the A-cluster and highlights some of the key issues regarding the electronic properties and reactivity of this cluster that need to be addressed in future studies.