biostudies-literature00570Hu YNIGMS NIH HHS753-5https://www.ebi.ac.uk/biostudies/studies/S-EPMC3153399biostudies-literatureUnknown333(6043)In a small-scale reaction, vanadium-dependent nitrogenase has previously been shown to catalyze reductive catenation of carbon monoxide (CO) to ethylene, ethane, propylene, and propane. Here, we report the identification of additional hydrocarbon products [α-butylene, n-butane, and methane (CH(4))] in a scaled-up reaction featuring 20 milligrams of vanadium-iron protein, the catalytic component of vanadium nitrogenase. Additionally, we show that the more common molybdenum-dependent nitrogenase can generate the same hydrocarbons from CO, although CH(4) was not detected. The identification of CO as a substrate for both molybdenum- and vanadium-nitrogenases strengthens the hypothesis that CO reduction is an evolutionary relic of the function of the nitrogenase family. Moreover, the comparison between the CO-reducing capacities of the two nitrogenases suggests that the identity of heterometal at the active cofactor site affects the efficiency and product distribution of this reaction.Science (New York, N.Y.)Extending the carbon chain: hydrocarbon formation catalyzed by vanadium/molybdenum nitrogenases.PMC3153399R01 GM067626-08GM 67626R01 GM067626Ribbe MWHu YLee CC57falseExtending the carbon chain: hydrocarbon formation catalyzed by vanadium/molybdenum nitrogenases.In a small-scale reaction, vanadium-dependent nitrogenase has previously been shown to catalyze reductive catenation of carbon monoxide (CO) to ethylene, ethane, propylene, and propane. Here, we report the identification of additional hydrocarbon products [α-butylene, n-butane, and methane (CH(4))] in a scaled-up reaction featuring 20 milligrams of vanadium-iron protein, the catalytic component of vanadium nitrogenase. Additionally, we show that the more common molybdenum-dependent nitrogenase can generate the same hydrocarbons from CO, although CH(4) was not detected. The identification of CO as a substrate for both molybdenum- and vanadium-nitrogenases strengthens the hypothesis that CO reduction is an evolutionary relic of the function of the nitrogenase family. Moreover, the comparison between the CO-reducing capacities of the two nitrogenases suggests that the identity of heterometal at the active cofactor site affects the efficiency and product distribution of this reaction.2011-01-01T00:00:00Z2011 Aug2024-11-09T04:06:18.345Z2019-03-27T03:07:51ZS-EPMC31533992181705310.1126/science.1206883