ATP-independent substrate reduction by nitrogenase P-cluster variant

作者：Lee Chi Chung; Hu Yilin^*; Ribbe Markus W

来源：Proceedings of the National Academy of Sciences of the United States of America, 2012, 109(18): 6922-6926.

DOI：10.1073/pnas.1202429109

• Fischer-Tropsch
• CN-
• CO
• CO2

The P-cluster of nitrogenase is largely known for its function to mediate electron transfer to the active cofactor site during catalysis. Here, we show that a P-cluster variant (designated P*-cluster), which consists of paired [Fe4S4]-like clusters, can catalyze ATP-independent substrate reduction in the presence of a strong reductant, europium (II) diethylenetriaminepentaacetate [Eu(II)-DTPA]. The observation of a decrease of activity in the rank Delta nifH, Delta nifB Delta nifZ, and Delta nifB MoFe protein, which corresponds to a decrease of the amount of P*-clusters in these cofactor-deficient proteins, firmly establishes P*-cluster as a catalytically active metal center in Eu(II)-DTPA-driven reactions. More excitingly, the fact that P*-cluster is not only capable of catalyzing the two-electron reduction of proton, acetylene, ethylene, and hydrazine, but also capable of reducing cyanide, carbon monoxide, and carbon dioxide to alkanes and alkenes, points to a possibility of developing biomimetic catalysts for hydrocarbon production under ambient conditions.

• 出版日期2012-5-1