Stephen Cramer

Stephen P. Cramer, whose research straddles the fields of synchrotron x-ray spectroscopy and bio-inorganic chemistry, is an Advanced Light Source Professor at UC Davis and Lawrence Berkeley National Laboratory. He became involved with synchrotron radiation in 1974, during thesis work on the EXAFS of nitrogenase at Stanford's SSRP. Following an NIH post-doc with Harry Gray, he joined Exxon Research, where he used EXAFS and other methods to characterize man-made and biological catalysts. Since then, he has worked on developing new synchrotron methods for characterizing metals in biology. These include the first bioinorganic applications of soft x-ray magnetic circular dichroism (XMCD) and resonant inelastic x-ray scattering (RIXS). More recently, his group has employed nuclear resonance vibrational spectroscopy (NRVS) and femtosecond pump probe spectroscopy (FPPS), as well conventional methods such as FT-IR, resonance Raman, and Mössbauer spectroscopy.

Education, Awards and Professional Highlights

• Eastern Analytical Symposium Award for Outstanding Achievements in Vibrational Spectroscopy (2018)
• Einstein Visiting Fellow Award, Einstein Foundation Berlin (2016)
• Humboldt Foundation Research Award (2014)
• American Association for the Advancement of Science Fellow (2013)
• New York Society for Applied Spectroscopy Gold Medal (2013)
• International X-Ray Absorption Society “Edward Stern Outstanding Achievement Award” (2012)
• American Chemical Society “Spectrochemical Analysis” Award (2010)
• Senior Faculty Scientist Physical Biosciences Division, Lawrence Berkeley Lab (1991-2014)
• Advanced Light Source Professor, UC Davis (1991-Present)
• Physicist, National Synchrotron Light Source, Brookhaven National Lab (1988-1990)
• Member of Professional Staff Schlumberger-Doll Research (1986-1988)
• Senior Staff Chemist and Group Head, Exxon Research (1978-1986)
• California Institute of Technology - NIH post-doc with Prof. Harry Gray (1978)
• Ph.D. Stanford University (1978)
• B.A. Williams College (1973)

Representative Publications

• "Direct observation of an iron bound terminal hydride intermediate in [FeFe] hydrogenase", Reijerse, E. J.; Pham, C. C.; Pelmenschikov, V.; Gilbert-Wilson, R.; Adamska-Venkatesh, A.; Siebel, J. F.; Gee, L. B.; Yoda, Y.; Tamasaku, K.; Lubitz, W.; Rauchfuss, T. B.; Cramer, S. P. J. Am. Chem. Soc., 2017, 139, 4306-4309.
• "Synchrotron-based Nickel Mössbauer Spectroscopy", Gee, L. B.; Lin, C.-Y.; Jr., F. E. J.; Yoda, Y.; Masuda, R.; Saito, M.; Kobayashi, Y.; Tamasaku, K.; Seto, M.; Charles G. Riordan; Ploskonka, A.; Power, P. P.; Cramer, S. P.; Lauterbach, L. Inorg. Chem., 2016, 55I, 6866–6872.
• "The Radical SAM Enzyme HydG Requires Cysteine and a Dangler Iron for Generating an Organometallic Precursor to the FeFe Hydrogenase H-Cluster", Suess, D. L. M.; Pham, C. C.; Bürstel, I.; Swartz, J. R.; Cramer, S.; Britt, R. D. J. Am. Chem. Soc., 2016, 138, 1146−1149.
• "Low Frequency Dynamics of Nitrogenase via Femtosecond Pump Probe Spectroscopy – Observation of a Candidate Promoting Vibration", Maiuri, M.; Delfino, I.; Cerullo, G.; Manzoni, C.; Pelmenschikov, V.; Guo, Y.; Wang, H.; Gee, L. B.; Dapper, C. H.; Newton, W. E.; Cramer, S. P. J.  Inorg. Biochem., 2016, 153, 128-135.
• "Cysteine as a ligand platform in the biosynthesis of the FeFe hydrogenase H cluster", Suess, D. L. M.; Bürstel, I.; Paz, L. D. L.; Kuchenreuther, J. M.; Pham, C. C.; Cramer, S. P.; Swartz, J. R.; Britt, R. D. Proc. Nat. Acad. Sci., 2015, 112, 11455-11460.
• "Spectroscopic Investigations of [FeFe] Hydrogenase Maturated with [57Fe2(adt)(CN)2(CO)4]2-", Gilbert-Wilson, R.; Siebel, J. F.; Pham, C. C.; Adamska-Venkatesh, A.; Reijerse, E.; Wang, H.; Cramer, S. P.; Lubitz, W.; Rauchfuss, T. B. J. Am. Chem. Soc., 2015, 137, 8998-9005.
• "Docking and Migration of Carbon Monoxide in Nitrogenase – The Case for Gated Pockets from IR Spectroscopy and Molecular Dynamics", Gee, L. B.; Leontyev, I.; Scott, A. D.; Pelmentschikov, V.; Stuchebrukhov, A.; Cramer, S. P. Biochemistry, 2015, 54, 3314-3319
• "IR-Monitored Photolysis of CO-Inhibited Nitrogenase: A Major EPR-Silent Species with Coupled Terminal CO Ligands", Yan, L.; Pelmenschikov, V.; Dapper, C. H.; Scott, A. D.; Newton, W. E.; Cramer, S. P. Chem. Eur. J., 2012, 18, 16349–16357.