DeBeer, Serena - Cornell University - Department of Chemistry and Chemical Biology

个人简介

Serena received her PhD in chemistry from Stanford University (under the direction of Edward I. Solomon and Keith O. Hodgson). She then accepted a position as a staff scientist at the SLAC National Accelerator Laboratory. In the Fall of 2009, she moved to Cornell as an assistant professor in the Department of Chemistry and Chemical Biology. Her research focuses on the development and application of synchrotron spectroscopies to understand fundamental questions in biological and chemical catalysis.

研究领域

Metalloenzymes are Nature's catalysts and are able to carry out remarkably difficult chemical transformations which often pose significant challenges in a laboratory setting (including the need for high temperatures, high pressures, and complex synthetic procedures). These enzymatic catalysts include nitrogenase (which converts dinitrogen to ammonia), the oxygen-evolving complex in photosystem II, and methane monooxygenase (which converts methane to methanol). In all these examples, a metal-based active site is the center of catalytic activity; and it is these transition metal active sites which have provided much inspiration for biomimetic model chemistry and for homogeneous catalysis, and are the focus of our research program. We are interested in development and application of X-ray based spectroscopies as probes of electronic structure in biological and chemical catalysis. We study both enzyme systems and small molecule model complexes, which aim to mimic the enzyme activity. In particular, we are interested in the development of new spectroscopic methods which enable the characterization of intermediates in reaction cycles and hence may provide experimental insight into mechanisms. Our primary efforts focus on X-ray absorption and X-ray emission spectroscopic studies, which will be carried out at the Cornell High Energy Synchrotron Source (CHESS), the Stanford Synchrotron Radiation Laboratory (SSRL) and other synchrotron facilities. These data will be complemented by more traditional spectroscopy (UV-Vis, EPR and vibrational data), as well as modern electronic structure calculations. Our research program provides students with training in advanced spectroscopic methods, data analysis, theoretical calculations and basic synthesis, as well as the opportunity to collaborate with experts in biochemistry, synthetic chemistry and theory.

近期论文

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“X-ray Absorption Spectra of the Oxidized and Reduced Forms of C112D Azurin fromPseudomonas aeruginosa.” S. DeBeer, C. N. Kiser, G. A. Mines, J. H. Richards, H. B. Gray, E. I.Solomon, B. Hedman and K. O. Hodgson. Inorg. Chem. 1999, 38, 433. “A Study of Solid [{Cu(MePY2)}2O22+ using Resonance Raman and X-ray AbsorptionSpectroscopies; an Intermediate Cu2O2 Core Structure or a Solid Solution?” E. Pidcock, S.DeBeer, H. V. Obias, B. Hedman, K. O. Hodgson, K. D. Karlin and E. I. Solomon. J. Am. Chem.Soc. 1999, 121, 1870. “X-ray Absorption Spectroscopy of Folded and Unfolded Copper (I) Azurin.” S. DeBeer,Pernilla Wittung-Stafshede, J. Leckner, G. Karlsson, J. R. Winkler, H. B. Gray, B. G.Malmström, E. I. Solomon, B. Hedman, K. O. Hodgson. Inorg. Chim. Acta (S. J. Lippard Issue)2000, 297, 278. “X-ray Absorption Edge and EXAFS Studies of the Blue Copper Site in Stellacyanin: Effectsof Axial Amide Coordination.” S. DeBeer, D. W. Randall, A. M. Nersissian, J. S. Valentine, B.Hedman, K. O. Hodgson, and E. I. Solomon J. Phys. Chem.(T. Spiro Issue), 2000, 104, 10814. “Spectroscopic and Electronic Structural Studies of Blue Copper Model Complexes. 2:Comparison of 3- and 4- Coordinate Cu(II) Thiolate Complexes and Fungal Laccase.”D. W.Randall, S. DeBeer George, P. L. Holland, K. O. Hodgson, W. B. Tolman, E. I. Solomon. J. Am. Chem. Soc., 2000, 122, 11632. “Spectroscopic and Electronic Structural Studies of Blue Copper Model Complexes. 1:Perturbation of the Thiolate-Cu Bond.” D. W. Randall, S. DeBeer George, B. Hedman, K. O.Hodgson, K. Fujisawa, and E. I. Solomon. J. Am Chem. Soc., 2000, 122, 11620. “Recent Advances in Bioinorganic Spectroscopy.” N. Lehnert, S. DeBeer George, E. I.Solomon. Current Opinion in Chemical Biology, 2001, 5, 176. “Raman and EXAFS Characterization of Sulfur-Ligand Cu(I) Ethylene Complex: A Model forthe Arabidopsis Ethylene Receptor.” J. Hirsch, S. DeBeer George, E. I. Solomon, B. Hedman, K.O. Hodgson and J. N. Burstyn. Inorg. Chem., 2001, 40, 2439. “A Quantitative Description of the Ground State Wave Function of CuA from X-ray AbsorptionSpectroscopy: Comparison to Plastocyanin and Relevance to Electron Transfer.” S. DeBeerGeorge, M. Metz, R. K. Szilagyi, H. Wang, S. P. Cramer, Y. Lu, W. B. Tolman, B. Hedman, K.O. Hodgson, E. I. Solomon. J. Am. Chem. Soc., 2001, 123, 5757. “Nature of the Intermediate Formed in the Reduction of O2 to H2O at the Trinuclear CopperCluster Active Site in Native Laccase.” S.-K. Lee, S. DeBeer George, W. E. Antholine, B.Hedman, K. O. Hodgson, E. I. Solomon, J. Am. Chem. Soc., 2002, 124, 6180. “Electronic Structure Description of the μ4-Sulfide Bridged Tetranuclear CuZ Center in N2OReductase.” P. Chen, S. DeBeer George, I. Cabrito, W. E. Antholine, J. J. G. Moura, I. Moura, B. Hedman, K. O. Hodgson, and E. I. Solomon, J. Am. Chem. Soc., 2002, 124, 744. "Spectroscopic Comparison of the Five-coordinate [Cu(SMeIm)(HB(3,5-iPr2pz)3)] with the Four-coordinate [Cu(SCPh3)(HB(3,5-iPr2pz)3)]: Effect of Coordination Number Increase on a Serena DeBeer Page 2 Copper Type Site" L. Basumallick, S. DeBeer George, D. W. Randall, B. Hedman, K. O. Hodgson, K. Fujisawa and E. I. Solomon, Inorg. Chim. Acta (K. Weighardt Issue) 2002, 337, 357. “Spectroscopic Investigation of Stellacyanin Mutants: Axial Ligand Interactions at the Blue Copper Site” S. DeBeer George, L. Basumallick, R. K. Szilagyi, D. W. Randall, M. G. Hill, A. M. Nersissian, J. S. Valentine, B. Hedman, K. O. Hodgson, E. I. Solomon. J. Am. Chem. Soc., 2003, 125, 11314. “Electronic Structures of Metal Sites in Proteins and Models: Contributions to Function in Blue Copper Proteins” E. I. Solomon, R. K. Szilagyi, S. DeBeer George, L. Basumallick, Chem. Rev., 2004, 104, 419. “High Covalence in CuSO4 and the Radicalization of Sulfate: An X-ray Absorption and Density Functional Study” P. Frank, R. K. Szilagyi, S. DeBeer George, Britt Hedman, Keith O. Hodgson, Inorg. Chem., 2004, 43, 8318. “Copper Proteins with Type 1 Sites” P. J. Hart, A. M. Nersissian, S. DeBeer George, In Encyclopedia of Inorganic Chemistry, 2nd Ed., Vol. II, King, R. B., Editor, Wiley:Chichester, 2005; pp 1173-1201. “Metal and Ligand K-Edge XAS of Organotitanium Complexes: Metal 4p and 3d Contributions to Pre-edge Intensity and Their Contributions to Bonding” S. DeBeer George, P. Brant, E. I. Solomon, J. Am. Chem. Soc., 2005, 127, 667. “Spectroscopic and Density Functional Studies of the Red Copper Site in Nitrosocyanin: Role of the Protein in Determining Active Site Geometric and Electronic Structure” L. Basumallick, R. Sarangi, S. DeBeer George, B. Elmore, A. B. Hooper, B. Hedman, K. O. Hodgson, E. I. Solomon, J. Am. Chem. Soc., 2005, 127, 3531. “The Geometric and Electronic Structure of [(cyclam-acetato)Fe(N)]+: A Genuine Iron(V) Species with a Ground-State Spin S=1/2” N. Aliaga-Alcalde, S. DeBeer George, B. Mienert, E. Bill, K. Wieghardt, F. Neese, Angew. Chem. Int. Ed., 2005, 44, 2908. “The Molecular and Electronic Structure of Oxo-bis(benzene-1,2-dithiolato)chromate(V) Monoanions. A Combined Experimental and Density Functional Study” K. Ray, R. Kapre, I. Sylvestre, T. Weyhermüller, S. DeBeer George, F. Neese, K. Wieghardt, Inorg. Chem., 2006, 45, 3499-3509. (cover article)