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- W2162608396 abstract "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 [Fe 4 S 4 ]-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 Δ nifH , Δ nifB Δ nifZ , and Δ 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." @default.
- W2162608396 created "2016-06-24" @default.
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- W2162608396 date "2012-04-16" @default.
- W2162608396 modified "2023-09-26" @default.
- W2162608396 title "ATP-independent substrate reduction by nitrogenase P-cluster variant" @default.
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- W2162608396 doi "https://doi.org/10.1073/pnas.1202429109" @default.
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