The enzyme carbon monoxide dehydrogenase is capable of efficiently converting \(\hbox {CO}_{2}\) to CO and, therefore, can enable an affordable \(\hbox {CO}_{2}\) recycling strategy. The reduction of \(\hbox {CO}_{2}\) occurs at a peculiar nickel–iron–sulfur cluster, following a mechanism that remains little understood. In this study, we have used ab initio molecular dynamics simulations to explore the free energy landscape of the reaction. We predict the existence of a COOH ligand that strongly interacts with the surrounding protein residues and favours a mechanism where a \(\hbox {H}_{2}\hbox {O}\) molecule is eliminated before CO. We have taken advantages of the insights offered by our simulations to revisit the catalytic mechanism and the role of the residues surrounding the active centre in particular, thus assisting in the design of inorganic catalysts that mimic the enzyme.

一氧化碳脱氢酶能够有效地将\(\hbox {CO}_{2}\)转化为 CO，因此可以实现经济实惠的\(\hbox {CO}_{2}\)回收策略。\(\hbox {CO}_{2}\)的还原发生在一个特殊的镍-铁-硫簇中，其机制仍然鲜为人知。在这项研究中，我们使用了从头分子动力学模拟来探索反应的自由能景观。我们预测存在与周围蛋白质残基强烈相互作用并支持\(\hbox {H}_{2}\hbox {O}\) 分子在 CO 之前被消除。我们利用模拟提供的见解重新审视催化机制和特别是活性中心周围残基的作用，从而帮助设计模拟酶的无机催化剂。