Prof. Dr. Stephen P. Cramer
Stephen P. Cramer is Professor of Chemistry at University of California, Davis.
As an Einstein Visiting Fellow Cramer conducts his research at the Einstein Center for Catalysis and the Cluster of Excellence “Unifying Concepts in Catalysis“ (UniCat).
In UniCat, he has joined the UniCat working group of Professor Peter Hildebrandt.
Professor Stephen P. Cramer from the University of California, Davis will join the UniCat research group of Professor Peter Hildebrandt as Einstein Visiting Fellow.
|2442 Spectroscopic and Computational Evidence that [FeFe] Hydrogenases Operate Exclusively with CO-Bridged Intermediates J. A. Birrell, V. Pelmenschikov, N. Mishra, H. Wang, Y. Yoda, K. Tamasaku, T. B. Rauchfuss, S. P. Cramer, W. Lubitz, S. DeBeer Journal of the American Chemical Society 2019, 1, 222–232, 10.1021/jacs.9b09745 |
|2431 Asymmetry in the Ligand Coordination Sphere of the [FeFe] Hydrogenase Active Site Is Reflected in the Magnetic Spin Interactions of the Aza-propanedithiolate Ligand E. J. Reijerse, V. Pelmenschikov, J. A. Birrell, C. P. Richers, M. Kaupp, T. B. Rauchfuss, S. P. Cramer, W. Lubitz The Journal of Physical Chemistry Letters 2019, 21, 6794–6799, 10.1021/acs.jpclett.9b02354 |
|2415 Insights from Te and Fe nuclear resonance vibrational spectroscopy: a [4Fe–4Te] cluster from two points of view F. Wittkamp, N. Mishra, H. Wang, H. C. Wille, R. Steinbrügge, M. Kaupp, S. P. Cramer, U. P. Apfel, V. Pelmenschikov Chemical Science 2019, 32, 7535–7541, 10.1039/C9SC02025J |
|2303 Terminal Hydride Species in [FeFe]-Hydrogenases Are Vibrationally Coupled to the Active Site Environment C. C. Pham, D. W. Mulder, V. Pelmenschikov, P. W. King, M. W. Ratzloff, H. Wang, N. Mishra, E. E. Alp, J. Zhao, M. Y. Hu, K. Tamasaku, Y. Yoda, S. P. Cramer Angewandte Chemie International Edition 2018, 33, 10605–10609, 10.1002/anie.201805144 |
|2301 High-Frequency Fe-H Vibrations in a Bridging Hydride Complex Characterized by NRVS and DFT V. Pelmenschikov, L. B. Gee, H. Wang, K. C. MacLeod, S. F. McWilliams, K. L. Skubi, S. P. Cramer, P. L. Holland Angewandte Chemie International Edition 2018, 30, 9367–9371, 10.1002/anie.201804601 |
|2229 Enzymatic and spectroscopic properties of a thermostable [NiFe]‑hydrogenase performing H2-driven NAD+-reduction in the presence of O2 J. Preissler, S. Wahlefeld, C. Lorent, C. Teutloff, M. Horch, L. Lauterbach, S. P. Cramer, I. Zebger, O. Lenz Biochimica et Biophysica Acta (BBA) - Bioenergetics 2018, 1, 8–18, 10.1016/j.bbabio.2017.09.006 |
|2172 Sterically Stabilized Terminal Hydride of a Diiron Dithiolate M. R. Carlson, D. L. Gray, C. P. Richers, W. Wang, P. H. Zhao, T. B. Rauchfuss, V. Pelmenschikov, C. C. Pham, L. B. Gee, H. Wang, S. P. Cramer Inorganic Chemistry 2018, 4, 1988–2001, 10.1021/acs.inorgchem.7b02903 |
|2146 Reaction Coordinate Leading to H Production in [FeFe]-Hydrogenase Identified by Nuclear Resonance Vibrational Spectroscopy and Density Functional Theory V. Pelmenschikov, J. A. Birrell, C. C. Pham, N. Mishra, H. Wang, C. Sommer, E. Reijerse, C. P. Richers, K. Tamasaku, Y. Yoda, T. B. Rauchfuss, W. Lubitz, S. P. Cramer Journal of the American Chemical Society 2017, 46, 16894–16902, 10.1021/jacs.7b09751 |
|2119 Direct Observation of an Iron-Bound Terminal Hydride in [FeFe]-Hydrogenase by Nuclear Resonance Vibrational Spectroscopy E. J. Reijerse, C. C. Pham, V. Pelmenschikov, R. Gilbert-Wilson, A. Adamska-Venkatesh, J. F. Siebel, L. B. Gee, Y. Yoda, K. Tamasaku, W. Lubitz, T. B. Rauchfuss, S. P. Cramer Journal of the American Chemical Society 2017, 12, 4306–4309, 10.1021/jacs.7b00686 |
|2016 Synchrotron-based Nickel Mössbauer Spectroscopy L. B. Gee, C. Y. Lin, F. E. Jenney, M. W. W. Adams, Y. Yoda, R. Masuda, M. Saito, Y. Kobayashi, K. Tamasaku, M. Lerche, M. Seto, C. G. Riordan, A. Ploskonka, P. P. Power, S. P. Cramer, L. Lauterbach Inorganic Chemistry 2016, 14, 6866–6872, 10.1021/acs.inorgchem.5b03004 |
|1926 Characterization of [4Fe-4S] Cluster Vibrations and Structure in Nitrogenase Fe Protein at Three Oxidation Levels via Combined NRVS, EXAFS, and DFT Analyses D. Mitra, S. J. George, Y. Guo, S. Kamali, S. Keable, J. W. Peters, V. Pelmenschikov, D. A. Case, S. P. Cramer Journal of the American Chemical Society 2013, 7, 2530–2543, 10.1021/ja307027n |
|1924 Low frequency dynamics of the nitrogenase MoFe protein via femtosecond pump probe spectroscopy — Observation of a candidate promoting vibration M. Maiuri, I. Delfino, G. Cerullo, C. Manzoni, V. Pelmenschikov, Y. Guo, H. Wang, L. B. Gee, C. H. Dapper, W. E. Newton, S. P. Cramer Journal of Inorganic Biochemistry Journal of Inorganic Biochemistry 2015, 128–135, 10.1016/j.jinorgbio.2015.07.005 |
|1922 Characterization of the [3Fe–4S] cluster from the D14C variant of Pyrococcus furiosus ferredoxin via combined NRVS and DFT analyses L. Lauterbach, L. B. Gee, V. Pelmenschikov, F. E. Jenney, S. Kamali, Y. Yoda, M. W. W. Adams, S. P. Cramer Dalton Transactions Dalton Trans. 2016, 17, 7215–7219, 10.1039/C5DT04760A |
|1692 Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy H. Ogata, T. Krämer, H. Wang, D. Schilter, V. Pelmenschikov, M. van Gastel, F. Neese, T. B. Rauchfuss, L. B. Gee, A. D. Scott, Y. Yoda, Y. Tanaka, W. Lubitz, S. P. Cramer Nature Communications Nature Communications 2015, 1, 10.1038/ncomms8890 |
|1683 Docking and Migration of Carbon Monoxide in Nitrogenase: The Case for Gated Pockets from Infrared Spectroscopy and Molecular Dynamics L. B. Gee, I. Leontyev, A. Stuchebrukhov, A. D. Scott, V. Pelmenschikov, S. P. Cramer Biochemistry 2015, 21, 3314–3319, 10.1021/acs.biochem.5b00216 |
|1638 Nuclear resonance vibrational spectroscopy reveals the FeS cluster composition and active site vibrational properties of an O -tolerant NAD -reducing [NiFe] hydrogenase L. Lauterbach, H. Wang, M. Horch, L. B. Gee, Y. Yoda, Y. Tanaka, I. Zebger, O. Lenz, S. P. Cramer Chemical Science Chem. Sci. 2015, 2, 1055–1060, 10.1039/C4SC02982H |
|1443 Structural Characterization of CO-Inhibited Mo-Nitrogenase by Combined Application of Nuclear Resonance Vibrational Spectroscopy, Extended X-ray Absorption Fine Structure, and Density Functional Theory: New Insights into the Effects of CO Binding and the Role of the Interstitial Atom A. D. Scott, V. Pelmenschikov, Y. Guo, L. Yan, H. Wang, S. J. George, C. H. Dapper, W. E. Newton, Y. Yoda, Y. Tanaka, S. P. Cramer Journal of the American Chemical Society 2014, 45, 15942–15954, 10.1021/ja505720m |
|1427 Synthesis and vibrational spectroscopy of Fe-labeled models of [NiFe] hydrogenase: first direct observation of a nickel–iron interaction D. Schilter, V. Pelmenschikov, H. Wang, F. Meier, L. B. Gee, Y. Yoda, M. Kaupp, T. B. Rauchfuss, S. P. Cramer Chem. Commun. Chem. Commun. 2014, 88, 13469–13472, 10.1039/C4CC04572F |
|1241 The HydG Enzyme Generates an Fe(CO)2(CN) Synthon in Assembly of the FeFe Hydrogenase H-Cluster J. M. Kuchenreuther, W. K. Myers, D. L. M. Suess, T. A. Stich, V. Pelmenschikov, S. A. Shiigi, S. P. Cramer, J. R. Swartz, R. D. Britt, S. J. George Science 2014, 6169, 424–427, 10.1126/science.1246572 |
|1144 IR-Monitored Photolysis of CO-Inhibited Nitrogenase: A Major EPR-Silent Species with Coupled Terminal CO Ligands L. Yan, V. Pelmenschikov, C. H. Dapper, A. D. Scott, W. E. Newton, S. P. Cramer Chemistry - A European Journal 2012, 51, 16349–16357, 10.1002/chem.201202072 |