Lance Seefeldt

Publications | Book Chapters

• Seefeldt, L., (2017). Nitrogen Fixation: Ullmann’s Encyclopedia of Industrial Chemistry. Wiley-VCH Verlag GmbH & Co. KGaA

An asterisk (*) at the end of a publication indicates that it has not been peer-reviewed.

Publications | Journal Articles

Academic Journal

• Badalyan, A., Yang, Z., Hu, M., Liu, T.L, Seefeldt, L., (2022). Tailoring electron transfer pathway for photocatalytic N2-to-NH3 reduction in a CdS quantum dots-nitrogenase system. Sustainable Energy Fuels, 6, 2256--2263.
• Badalyan, A., Yang, Z., Hu, B., Luo, J., Hu, M., Liu, T.L, Seefeldt, L., (2019). An Efficient Viologen-Based Electron Donor to Nitrogenase. Biochemistry, 58, 4590-4595.
• Hu, B., Hu, M., Seefeldt, L., Liu, T.L, (2019). Electrochemical Dinitrogen Reduction to Ammonia by Mo2N: Catalysis or Decomposition?. ACS Energy Lett., 4:5, 1053--1054.
• Peters, J.W, Beratan, D.N, Bothner, B., Dyer, R.B, Harwood, C.S, Heiden, Z.M, Hille, R., Jones, A.K, King, P.W, Lu, Y., Lubner, C.E, Minteer, S.D, Mulder, D.W, Raugei, S., Schut, G.J, Seefeldt, L., Tokmina-Lukaszewska, M., Zadvornyy, O.A, Zhang, P., Adams, M.W, (2018). A new era for electron bifurcation. Curr. Opin. Chem. Biol., 47, 32--38.
• Zheng, Y., Harris, D.F, Yu, Z., Fu, Y., Poudel, S., Ledbetter, R.N, Fixen, K.R, Yang, Z., Boyd, E.S, Lidstrom, M.E, Seefeldt, L., Harwood, C.S, (2018). A pathway for biological methane production using bacterial iron-only nitrogenase. Nature Microbiology, 3, 281--286.
• Chen, J.G, Crooks, R.M, Seefeldt, L., Bren, K.L, Bullock, R.M, Darensbourg, M.Y, Holland, P.L, Hoffman, B., Janik, M.J, Jones, A.K, Kanatzidis, M.G, King, P., Lancaster, K.M, Lymar, S.V, Pfromm, P., Schneider, W.F, Schrock, R.R, (2018). Beyond fossil fuel–driven nitrogen transformations. Science, 360:6391, eaar6611.
• Mao, Z., Liou, S., Khadka, N., Jenney, F.E, Goodin, D.B, Seefeldt, L., Adams, M.W, Cramer, S., Larsen, D.S, (2018). Cluster Dependent Charge-Transfer Dynamics in Iron-Sulfur Proteins. Biochemistry, 57, 978--990.
• Seefeldt, L., Peters, J.W, Beratan, D.N, Bothner, B., Minteer, S.D, Raugei, S., Hoffman, B.M, (2018). Control of electron transfer in nitrogenase. Curr. Opin. Chem. Biol., 47, 54--59.
• Raugei, S., Seefeldt, L., Hoffman, B.M, (2018). Critical computational analysis illuminates the reductive-elimination mechanism that activates nitrogenase for N2 reduction. PNAS, 201810211.
• Hu, B., Harris, D., Dean, D., Liu, T.L, Yang, Z., Seefeldt, L., (2018). Electrocatalytic CO2 Reduction Catalyzed by Nitrogenase MoFe and FeFe Proteins. Bioelectrochemistry, 120, 104-109.
• Poudel, S., Colman, D.R, Fixen, K.R, Ledbetter, R.N, Zheng, Y., Pence, N., Seefeldt, L., Peters, J.W, Harwood, C.S, Boyd, E.S, (2018). Electron transfer to nitrogenase in different genomic and metabolic backgrounds. J. Bacteriol., 200, JB.00757--17.
• Seefeldt, L., Hoffman, B.M, Peters, J.W, Raugei, S., Beratan, D.N, Antony, E., Dean, D.R, (2018). Energy transduction in nitrogenase. Acc. Chem. Res., 51, 2179--2186.
• Mus, F., Alleman, A.B, Pence, N., Seefeldt, L., Peters, J.W, (2018). Exploring the alternatives of biological nitrogen fixation. Metallomics, 10:4, 523--538.
• Lukoyanov, D.A, Khadka, N., Yang, Z., Dean, D.R, Seefeldt, L., Hoffman, B.M, (2018). Hydride Conformers of the Nitrogenase FeMo-cofactor Two-Electron Reduced State E2(2H), Assigned Using Cryogenic Intra Electron Paramagnetic Resonance Cavity Photolysis. Inorg. Chem., 57, 6847--6852.
• Harris, D., Yang, Z., Dean, D.R, Seefeldt, L., Hoffman, B.M, (2018). Kinetic Understanding of N2 Reduction versus H2 Evolution at the E4(4H) Janus State in the Three Nitrogenases. Biochemistry, 57, 5706--5714.
• Harris, D.F, Lukoyanov, D.A, Shaw, S., Compton, P., Tokmina-Lukaszewska, M., Bothner, B., Kelleher, N., Dean, D.R, Hoffman, B.M, Seefeldt, L., (2018). Mechanism of N2 reduction catalyzed by Fe-nitrogenase involves reductive elimination of H$_{\textrm{2}}$. Biochemistry, 57, 70--710.
• Jimenez-Vicente, E., Yang, Z., Ray, W.K, Echavarri-Erasun, C., Cash, V.L, Rubio, L.M, Seefeldt, L., Dean, D.R, (2018). Sequential and differential interaction of assembly factors during nitrogenase MoFe protein maturation. J. Biol. Chem., 293, 9182--9823.
• Keable, S.M, Zadvornyy, O.A, Johnson, L.E, Ginovska, B., Rasmussen, A.J, Danyal, K., Eilers, B.J, Prussia, G.A, LeVan, A.X, Raugei, S., Seefeldt, L., Peters, J.W, (2018). Structural characterization of the P $^{\textrm{1+}}$ intermediate state of the P-cluster of nitrogenase. J. Biol. Chem., 293, 9629--9635.
• Harris, D., Lukoyanov, D., Shaw, S., Compton, P.D, Tokmina-Lukaszewska, M., Bothner, B., Kelleher, N.L, Dean, D.R, Hoffman, B.M, Seefeldt, L., (2017). The Mechanism of N2 Reduction Catalyzed by Fe-Nitrogenase Involves Reductive Elimination of H2. Biochemistry
• Costas, A.M, Poudel, S., Miller, A., Schut, G.J, Ledbetter, R.N, Fixen, K.R, Seefeldt, L., Adams, M.W, Harwood, C.S, Boyd, E.S, Peters, J.W, (2017). Defining Electron Bifurcation in the Electron-Transferring Flavoprotein Family. Journal of Bacteriology, 199:21, e00440–17.
• Khadka, N., Milton, R.D, Shaw, S., Lukoyanov, D., Dean, D.R, Minteer, S.D, Raugei, S., Hoffman, B.M, Seefeldt, L., (2017). Mechanism of Nitrogenase H2 Formation by Metal-Hydride Protonation Probed by Mediated Electrocatalysis and H/D Isotope Effects. Journal of the American Chemical Society, 139, 13518–13524.
• Pence, N., Tokmina-Lukaszewska, M., Yang, Z., Ledbetter, R.N, Seefeldt, L., Bothner, B., Peters, J.W, (2017). Unraveling the interactions of the physiological reductant flavodoxin with the different conformations of the Fe protein in the nitrogenase cycle. Journal of Biological Chemistry, jbc.M117.801548.
• Ledbetter, R., Garcia-Costas, A.M, Lubner, C.E, Mulder, D.W, Tokmina-Lukaszewska, M., Artz, J.H, Patterson, A., Magnuson, T., Jay, Z.J, Duan, H.D, Miller, J., Plunkett, M.H, Hoben, J.P, Barney, B.M, Carlson, R.P, Miller, A., Bothner, B., King, P.W, Peters, J.W, Seefeldt, L., (2017). The Electron Bifurcating FixABCX Protein Complex from Azotobacter vinelandii: Generation of Low-Potential Reducing Equivalents for Nitrogenase Catalysis. Biochemistry, 56, 4177–4190.
• Lukoyanov, D., Khadka, N., Dean, D.R, Raugei, S., Seefeldt, L., Hoffman, B.M, (2017). Photoinduced reductive elimination of H₂ from the nitrogenase dihydride (Janus) state involves a FeMo-cofactor-H₂ intermediate. Inorganic Chemistry, 56:4, 2233–2240.
• Davydov, R., Khadka, N., Yang, Z., Fielding, A.J, Lukoyanov, D., Dean, D.R, Seefeldt, L., Hoffman, B.M, (2016). Exploring electron/proton transfer and conformational changes in the nitrogenase MoFe protein and FeMo-cofactor through cryoreduction/EPR measurements. Israel Journal of Chemistry, 56, 841–851.
• Danyal, K., Shaw, S., Page, T.R, Duval, S., Horitani, M., Marts, A.R, Lukoyanov, D., Dean, D.R, Raugei, S., Hoffman, B.M, Seefeldt, L., Antony, E., (2016). Negative cooperativity in the nitrogenase Fe protein electron delivery cycle. Proceedings of the National Academy of Sciences, 113, E5783–E5791.
• Khadka, N., Dean, D.R, Smith, D., Hoffman, B.M, Raugei, S., Seefeldt, L., (2016). CO₂ reduction catalyzed by nitrogenase: pathways to formate, carbon monoxide, and methane. Inorganic Chemistry, 55:17, 8321–8330.
• Fixen, K.R, Zheng, Y., Harris, D.F, Shaw, S., Yang, Z., Dean, D.R, Seefeldt, L., Harwood, C.S, (2016). Light-driven carbon dioxide reduction to methane by nitrogenase in a photosynthetic bacterium. Proceedings of the National Academy of Sciences, 113:36, 10163–10167.
• Milton, R.D, Abdellaoui, S., Khadka, N., Dean, D.R, Leech, D., Seefeldt, L., Minteer, S.D, (2016). Nitrogenase bioelectrocatalysis: heterogeneous ammonia and hydrogen production by MoFe protein. Energy & Environmental Science, 9:8, 2550–2554.
• Lukoyanov, D., Khadka, N., Yang, Z., Dean, D.R, Seefeldt, L., Hoffman, B.M, (2016). Reductive elimination of H₂ activates nitrogenase to reduce the N≡N triple bond: characterization of the E4(4H) Janus intermediate in wild-type enzyme. Journal of the American Chemical Society, 138:33, 10674–10683.
• Yang, Z., Ledbetter, R., Shaw, S., Pence, N., Tokmina-Lukaszewska, M., Eilers, B., Guo, Q., Pokhrel, N., Cash, V.L, Dean, D.R, Antony, E., Bothner, B., Peters, J.W, Seefeldt, L., (2016). Evidence that the Pi release event is the rate-limiting step in the nitrogenase catalytic cycle. Biochemistry, 55, 3625–3635.
• Brown, K.A, Harris, D.F, Wilker, M.B, Rasmussen, A., Khadka, N., Hamby, H., Keable, S., Dukovic, G., Peters, J.W, Seefeldt, L., King, P.W, (2016). Light-driven dinitrogen reduction catalyzed by a CdS:nitrogenase MoFe protein biohybrid. Science, 352:6284, 448–450.
• Lukoyanov, D., Khadka, N., Yang, Z., Dean, D.R, Seefeldt, L., Hoffman, B.M, (2016). Reversible photoinduced reductive elimination of H₂ from the nitrogenase dihydride state, the E4(4H) Janus intermediate. Journal of the American Chemical Society, 138:4, 1320–1327.
• Lukoyanov, D., Yang, Z., Khadka, N., Dean, D.R, Seefeldt, L., Hoffman, B.M, (2015). Identification of a Key Catalytic Intermediate Demonstrates That Nitrogenase Is Activated by the Reversible Exchange of N2 for H2. Journal of the American Chemical Society
• Shaw, S., Lukoyanov, D., Danyal, K., Dean, D.R, Hoffman, B.M, Seefeldt, L., (2014). Nitrite and Hydroxylamine as Nitrogenase Substrates: Mechanistic Implications for the Pathway of N2 Reduction. Journal of the American Chemical Society, 136:36, 12776–12783.
• Hoffman, B.M, Lukoyanov, D., Yang, Z., Dean, D.R, Seefeldt, L., (2014). Mechanism of nitrogen fixation by nitrogenase: the next stage. Chemical Reviews, 114:8, 4041–4062.
• Smith, D., Danyal, K., Raugei, S., Seefeldt, L., (2014). Substrate channel in nitrogenase revealed by a molecular dynamics approach. Biochemistry, 53:14, 2278–2285.
• Lukoyanov, D., Yang, Z., Duval, S., Danyal, K., Dean, D.R, Seefeldt, L., Hoffman, B.M, (2014). A confirmation of the quench-cryoannealing relaxation protocol for identifying reduction states of freeze-trapped nitrogenase intermediates. Inorganic Chemistry, 53, 3688–3693.
• Adams, C., Godfrey, V., Wahlen, B., Seefeldt, L., Bugbee, B.G, (2013). Understanding precision nitrogen stress to optimize the growth and lipid content tradeoff in oleaginous green microalgae. Bioresource technology, 131, 188–194.
• Wahlen, B.D, Morgan, M.R, McCurdy, A.T, Willis, R.M, Morgan, M.D, Dye, D.J, Bugbee, B.G, Wood, B.D, Seefeldt, L., (2012). Biodiesel from microalgae, yeast, and bacteria: engine performance and exhaust emissions. Energy & Fuels, 27:1, 220–228.
• Wahlen, B.D, Willis, R.M, Seefeldt, L., (2011). Biodiesel production by simultaneous extraction and conversion of total lipids from microalgae, cyanobacteria, and wild-mixed cultures. Bioresource Technology, 102, 2724-2730.
• Yang, Z.Y, Seefeldt, L., Dean, D.R, Cramer, S.P, George, S.J, (2011). Steric control of the Hi-CO MoFe nitrogenase complex revealed by stopped-flow infra-red spectroscopy. Angewandte Chemie International Edition, 50, 272-275.
• Danyal, K., Mayweather, D., Dean, D.R, Seefeldt, L., Hoffman, B.M, (2010). Conformational gating of electron transfer from nitrogenase Fe protein to MoFe protein. Journal of the American Chemical Society, 132, 6894-6895.
• Sarma, R., Barney, B.M, Keable, S., Dean, D.R, Seefeldt, L., Peters, J.W, (2010). Insights into substrate binding at FeMo-cofactor in nitrogenase from the structure of an alpha70Ile MoFe protein variant. Journal of Inorganic Biochemistry, 104, 385-389.
• Lukoyanov, D., Yang, Z.Y, Dean, D.R, Seefeldt, L., Hoffman, B.M, (2010). Is Mo involved in hydride binding by the four-electron reduced (E4) intermediate of the nitrogenase MoFe protein? . Journal of the American Chemical Society, 132, 2526-2527.
• Danyal, K., Inglet, B.S, Vincent, K.A, Barney, B.M, Hoffman, B.M, Armstrong, F.A, Dean, D.R, Seefeldt, L., (2010). Uncoupling nitrogenase: catalytic reduction of hydrazine to ammonia by a MoFe protein in the absence of Fe protein-ATP. Journal of the American Chemical Society, 132, 13197-13199.
• Barney, B.M, Yurth, M.G, Dos Santos, P.C, Dean, D.R, Seefeldt, L., (2009). A substrate channel in the nitrogenase MoFe protein. Journal of Biological Inorganic Chemistry, 14, 1015-1022.
• Harris, D.G, Seefeldt, L., (2009). An Updated Kinetic Study of the Enzyme Lactase for the Biochemistry Laboratory. Journal of Chemical Education, 86, 271.
• Hoffman, B.M, Dean, D.R, Seefeldt, L., (2009). Climbing nitrogenase: towards a mechanism of enzymatic nitrogen fixation. Accounts of Chemical Research, 42, 609-619.
• Seefeldt, L., Hoffman, B.M, Dean, D.R, (2009). Mechanism of Mo-dependent nitrogenase. Annual Review of Biochemistry, 78, 101-722.
• Wahlen, B.D, Oswald, W.S, Seefeldt, L., Barney, B.M, (2009). Purification, characterization, and potential bacterial wax ester production role of an NADPH-dependent fatty aldehyde reductase from Marinobacter aquaeolei VT8 . Applied and Environmental Microbiology, 75, 2758-2764.
• Barney, B.M, Lukoyanov, D., Igarashi, R.Y, Laryukhin, M., Yang, T.C, Dean, D.R, Hoffman, B.M, Seefeldt, L., (2009). Trapping an intermediate of dinitrogen (N2) reduction on nitrogenase. Biochemistry, 48, 9094-9102.
• Sarma, R., Barney, B.M, Hamilton, T.L, Jones, A., Seefeldt, L., Peters, J.W, (2008). Crystal structure of the L protein of Rhodobacter sphaeroides light dependent protochlorophyllide reductase with MgADP bound: a homologue of the nitrogenase Fe protein. Biochemistry, 47, 13004-13015.
• Wahlen, B.D, Barney, B.M, Seefeldt, L., (2008). Synthesis of biodiesel from mixed feedstocks and longer chain alcohols using an acid catalyzed method. Energy Fuels, 22, 4223-4228.
• Seefeldt, L., (2008). Synthesis of Biodiesel from Mixed Feedstocks and Longer Chain Alcohols using an Acid Catalyzed Method. Energy and Fuels, 22, 4223.

Professional Journal

• Wahlen, B.D, Morgan, M.R, McCurdy, A.T, Willis, R.M, Dye, D.J, Bugbee, B.G, Wood, B.D, Seefeldt, L., (2013). Biodiesel from microalgae, yeast, and bacteria: engine performance and exhaust emissions. Energy Fuels, 27, 220-228.
• Duval, S., Danyal, K., Shaw, S., Lytle, A.K, Dean, D.R, Hoffman, B.M, Antony, E., Seefeldt, L., (2013). Electron transfer precedes ATP hydrolysis during nitrogenase catalysis. Proc. Natl. Acad. Sci. USA, 110, 16414-16419.
• Appel, A.M, Seefeldt, L., (2013). Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO2 Fixation.. Chem. Rev., 113, 6621-6658.
• Seefeldt, L., Yang, Z.Y, Duval, S., Dean, D.R, (2013). Nitrogenase reduction of carbon-containing compounds. Biochim. Biophys. Acta, 1827, 1102-1111.
• Hoffman, B.M, Lukoyanov, D., Dean, D.R, Seefeldt, L., (2013). Nitrogenase: a draft mechanism. Acc Chem Res, 46, 587-595.
• Yang, Z.Y, Khadka, N., Lukoyanov, D., Hoffman, B.M, Dean, D.R, Seefeldt, L., (2013). On reversible H2 loss upon N2 binding to FeMo-cofactor of nitrogenase. Proc. Natl. Acad. Sci. USA, 110, 16327-16332.
• Moure, V.R, Danyal, K., Wendroth, S., Muller-Santos, M., Pedrosa, F.O, Scarduelli, M., Souza, E.M, Seefeldt, L., (2013). The nitrogenase regulatory enzyme dinitrogenase reductase ADP-ribosyltransferase (DraT) is activated by direct interaction with the signal transduction protein GlnB. J. Bacteriol., 195, 279-286.
• Adams, C., Godfrey, V., Wahlen, B., Seefeldt, L., Bugbee, B.G, (2013). Understanding precision nitrogen stress to optimize the growth and lipid content tradeoff in oleaginous green microalgae. Bioresource Technol., 131, 188-194.
• Yang, Z.Y, Moure, V.R, Dean, D.R, Seefeldt, L., (2012). Carbon dioxide reduction to methane and coupling with acetylene to form propylene catalyzed by remodeled nitrogenase. Proc. Natl. Acad. Sci. USA, 109, 19644-19648.
• Barney, B.M, Wahlen, B.D, Garner, E., Wei, J., Seefeldt, L., (2012). Differences in substrate specificities of five bacterial was ester synthases. Appl. Environ. Microbiol., 78, 5734-5745.
• Seefeldt, L., Hoffman, B.M, Dean, D.R, (2012). Electron transfer in nitrogenase catalysis. Curr. Opin. Chem. Biol. , 16, 19-25.
• George, S.J, Barney, B.M, Mitra, D., Igarashi, R.Y, Guo, Y., Dean, D.R, Cramer, S.P, Seefeldt, L., (2012). EXAFS and NRVS reveal a conformational distortion of the FeMo-cofactor in the MoFe nitrogenase propargyl alcohol complex. . J. Inorg. Biochem., 112, 85-92.
• Mayweather, D., Danyal, K., Dean, D.R, Seefeldt, L., Hoffman, B.M, (2012). Temperature invariance of the nitrogenase electron transfer mechanism. Biochemistry, 51, 8391-8398.
• Lukoyanov, D., Yang, Z.Y, Barney, B.M, Dean, D.R, Seefeldt, L., Hoffman, B.M, (2012). Unification of reaction pathway and kinetic scheme for N2 reduction catalyzed by nitrogenase. Proc. Natl. Acad. Sci. USA, 109, 5583-5587.
• Doan, P.E, Telser, J., Barney, B.M, Igarashi, R.Y, Dean, D.R, Seefeldt, L., Hoffman, B.M, (2011). (57)Fe ENDOR spectroscopy and 'electron inventory' analysis of the nitrogenase E(4) intermediate suggest the metal-ion core of FeMo-cofactor cycles through only one redox couple. J. Am. Chem. Soc., 133, 17329-17340.
• Danyal, K., Dean, D.R, Hoffman, B.M, Seefeldt, L., (2011). ) Electron transfer within nitrogenase: evidence for a deficit spending mechanism. Biochemistry, 50, 9255-9263.
• Willis, R.M, Wahlen, B.D, Seefeldt, L., Barney, B.M, (2011). Characterization of a fatty acyl-CoA reductase from Marinobacter aquaeolei VT8: A bacterial enzyme catalyzing the reduction of fatty acyl-CoA to fatty alcohol. Biochemistry, 50, 10550-10558.
• Lukoyanov, D., Dkianov, S.A, Yang, Z.H, Barney, B.M, Samoilova, R.I, Narasimhulu, K., Dean, D.R, Seefeldt, L., Hoffman, B.M, (2011). ENDOR/HYSCORE studies of the common intermediate trapped during nitrogenase reduction of N2H2, CH3N2H, and N2H4 support an alternating reaction pathway for N2 reduction. J. Am. Chem. Soc., 133, 11655-11664.
• Yang, Z., Dean, D.R, Seefeldt, L., (2011). Molybdenum nitrogenase catalyzes the reduction and coupling of CO to form hydrocarbons. J. Biol. Chem., 286, 19417-19421.

An asterisk (*) at the end of a publication indicates that it has not been peer-reviewed.

Publications | Technical Reports

AES Reports

Research Reports

Other Reports

• Lehnert, N., Corruzzi, G., Hegg, E., Seefeldt, L., Stein, L.Y, Norton, J.M, (2016). Feeding the world in the 21st century: Grand challenges in the nitrogen cycle. National Science Foundation

An asterisk (*) at the end of a publication indicates that it has not been peer-reviewed.

Publications | Other

An asterisk (*) at the end of a publication indicates that it has not been peer-reviewed.