Lab Fellow, Joint Appointment
Lab Fellow, Joint Appointment

Dr. Lance Seefeldt joined Pacific Northwest National Laboratory in 2013 as a Joint Appointment from Utah State University.  He is working in the Physical and Computational Sciences Directorate’s Physical Sciences Division, in the Catalysis Science group.  He is working on an Office of Science Basic Energy Sciences project focused on understanding catalytic principles at the core of the precise energy, mass flow and reactivity in enzymes.

Dr. Seefeldt is  Professor of Biochemistry at Utah State University's College of Science. His full biography is available on USU's website.

PNNL Publications

2017

  • Khadka N., R.D. Milton, S. Shaw, D. Lukoyanov, D.R. Dean, S.D. Minteer, and S. Raugei, et al. 2017. "Mechanism of Nitrogenase H-2 Formation by Metal-Hydride Protonation Probed by Mediated Electrocatalysis and H/D Isotope Effects." Journal of the American Chemical Society139, no. 38:13518-13524. PNNL-SA-128474. doi:10.1021/jacs.7b07311
  • Lukoyanov D., N. Khadka, D.R. Dean, S. Raugei, L.C. Seefeldt, and B. Hoffman. 2017. "Photoinduced Reductive Elimination of H2 from the Nitrogenase Dihydride (Janus) State Involves a FeMo-cofactor-H2 Intermediate." Inorganic Chemistry 56, no. 4:2233-2240. PNNL-SA-123286. doi:10.1021/acs.inorgchem.6b02899

2016

  • Danyal K., S. Shaw, T.R. Page, S.S. Duval, M. Horitani, A.R. Marts, and D. Lukoyanov, et al. 2016. "Negative cooperativity in the nitrogenase Fe protein electron delivery cycle." Proceedings of the National Academy of Sciences of the United States of America 113, no. 40:E5783-E5791. PNNL-SA-111505. doi:10.1073/pnas.1613089113

2015

  • Danyal K., A.J. Rasmussen, S.M. Keable, B.S. Inglet, S. Shaw, O. Zadvornyy, and S.S. Duval, et al. 2015. "Fe Protein-Independent Substrate Reduction by Nitrogenase MoFe Protein Variants." Biochemistry 54, no. 15:2456-2462. PNNL-SA-108124. doi:10.1021/acs.biochem.5b00140

2014

  • Smith D.M., K. Danyal, S. Raugei, and L.C. Seefeldt. 2014. "Substrate Channel in Nitrogenase Revealed by a Molecular Dynamics Approach." Biochemistry 53, no. 14:2278-2285. PNNL-SA-98485. doi:10.1021/bi401313j