Document Type


Journal/Book Title


Publication Date



American Chemical Society

Award Number

NSF, Division of Chemistry (CHE) 1847674


NSF, Division of Chemistry (CHE)





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Last Page



Nitrogenase catalyzes the reduction of N2 to NH3, supporting all biological nitrogen fixation. Electron donors to this enzyme are ferredoxin or flavodoxin (in vivo) and sodium dithionite (in vitro). Features of these electron donors put a limit on spectrophotometric studies and electrocatalytic applications of nitrogenase. Although it is common to use methyl viologen as an electron donor for many low-potential oxidoreductases, decreased nitrogenase activity is observed with an increasing concentration of methyl viologen, limiting its utility under many circumstances. In this work, we suggest that this concentration-dependent decrease in activity can be explained by the formation of a dimer of the radical cation of methyl viologen (Me2V•+)2 at higher methyl viologen concentrations. In addition, viologens functionalized with positively and negatively charged groups were synthesized and studied using spectroscopy and cyclic voltammetry. A sulfonated viologen derivative, 1,1′-bis(3-sulfonatopropyl)-4,4′-bipyridinium radical {[(SPr)2V]}, was found to support full nitrogenase activity up to a mediator concentration of 3 mM, while the positively charged viologen derivative was not an efficient reductant of nitrogenase due to the high standard redox potential. The utility of [(SPr)2V] as an electron donor for nitrogenase was demonstrated by a simple, sensitive spectrophotometric assay for nitrogenase activity that can provide accurate values for the specific activity and turnover rate constant under argon. Under N2, the formation of ammonia was confirmed. Because of the observed full activity of nitrogenase and low overpotential, [(SPr)2V] should also prove to be valuable for nitrogenase electrocatalysis, including bioelectrosynthetic N2 reduction.

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