The Fe protein of nitrogenase contains a redox active [Fe₄S₄] cluster that plays a key role in electron transfer and substrate reduction. Here we show that the Fe protein of Methanosarcina acetivorans can reduce CO₂ and CO to hydrocarbons under ambient conditions. Further, we demonstrate that this reactivity is inherent to [Fe₄S₄] clusters, showing the ability of a synthetic [Fe₄S₄] compound to catalyse the same ambient reaction in solutions. Theoretical calculations suggest a reaction mechanism involving an aldehyde-like intermediate that gives rise to hydrocarbon products upon proton-coupled electron transfer and concomitant removal of water molecules. These results provide a framework for mechanistic investigations of FeS-based activation and reduction of CO₂ and CO while facilitating potential development of FeS catalysts capable of ambient conversion of CO₂ and CO into fuel products.

固氮酶的Fe蛋白包含氧化还原活性[Fe ₄ S ₄ ]簇，该簇在电子转移和底物还原中起关键作用。在这里，我们显示了乙草甲烷菌的铁蛋白可以在环境条件下将CO ₂和CO还原为碳氢化合物。此外，我们证明了此反应性是[Fe ₄ S ₄ ]团簇固有的，表明了合成的[Fe ₄ S ₄化合物催化溶液中相同的环境反应。理论计算表明，涉及一种醛类中间体的反应机理，该中间体在质子偶联的电子转移和水分子的去除作用下产生烃类产物。这些结果为基于FeS的活化和CO ₂和CO的还原的机理研究提供了框架，同时促进了潜在的FeS催化剂的潜在开发，该FeS催化剂能够将CO ₂和CO环境转化为燃料。