Bioenergetics and Engineering of Proteins, CNRS, UPR 9036, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.
J Am Chem Soc. 2011 Feb 23;133(7):2096-9. doi: 10.1021/ja110627b. Epub 2011 Jan 27.
Carbon monoxide is often described as a competitive inhibitor of FeFe hydrogenases, and it is used for probing H(2) binding to synthetic or in silico models of the active site H-cluster. Yet it does not always behave as a simple inhibitor. Using an original approach which combines accurate electrochemical measurements and theoretical calculations, we elucidate the mechanism by which, under certain conditions, CO binding can cause permanent damage to the H-cluster. Like in the case of oxygen inhibition, the reaction with CO engages the entire H-cluster, rather than only the Fe(2) subsite.
一氧化碳通常被描述为铁铁氢化酶的竞争性抑制剂，它被用于探测 H2 与活性位点 H 簇的合成或计算机模型的结合。然而，它并不总是表现为简单的抑制剂。我们采用一种结合了精确电化学测量和理论计算的原创方法，阐明了在某些条件下 CO 结合如何导致 H 簇永久性损坏的机制。与氧抑制的情况一样，与 CO 的反应涉及整个 H 簇，而不仅仅是 Fe(2)亚位点。
