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Scott Gronert

Professor Organic and biological/biophysical chemistry (804) 828-8551 sgronert@vcu.edu

Education
B.S., California State University, Long Beach, 1983
Ph.D., University of California, Berkeley, 1987
Postdoctoral, University of Colorado, 1987-90

Research interests
Research in the Gronert group focuses on using mass spectrometry and computational chemistry to investigate problems in organic and biological chemistry. Both of these techniques are evolving rapidly and proving to be two of the most powerful tools in modern chemistry.  

Gas-phase reaction mechanisms
Although the great majority of organic chemistry is carried out in solution, the gas-phase provides many advantages in probing reaction mechanisms. First, it is possible to study reactions in a well-characterized, inert environment and probe intermediates that are too reactive to isolate or characterize in solution. Second, in the absence of solvation and ion pairing effects, it is possible to investigate the intrinsic reaction mechanism and confidently attribute reactivity trends to the characteristics of the reaction partners. Moreover, differences between gas-phase and solution reactions offer important insights into the role of solvent in the reaction mechanism. Current projects focus on substitution vs. elimination reactions, chiral recognition in small molecular clusters, and oxidation mechanisms involving metal-centered catalysts.

Protein post-translational modifications
Post-translational protein modifications, such as phosphorylation and glycosylation, play a major role in signaling and other cellular activities, but remain a major challenge in modern bioanalytical chemistry. They are not coded by DNA, often are found in low concentrations and can be transient. Mass spectrometry and proteomics approaches have proven to be the prime tools for identifying and characterizing post-translational protein modifications. We are focusing our efforts on the identification of protein oxidation products related to aging and diabetes. In each case, cellular oxidative stress leads to irreversible protein modifications. In aging, protein carbonyls are formed and reach high concentrations late in life. In diabetes, hyperglycemia combined with oxidative stress eventually leads to advanced glycation end-products, a protein modification linked to several diseases. In our work, we are developing methods to identity the specific site and extent of the protein modification. Our approach involves selective labeling of the modification site followed by a proteomics analysis using mass spectrometry.

Selected references:

1. Gronert, S. “Quadrupole Ion Trap Studies of Fundamental Organic Reactions,” Mass Spectrom. Rev. 2005, 24, 100-120.
2. Gronert, S.; Keeffe, J. “Identity Hydride-Ion Transfer from C-H Donors to C Acceptor Sites. Enthalpies of Hydride Addition and Enthalpies of Activation. Comparison With C...H...C Proton Transfer. An ab initio Study,” J. Am. Chem. Soc., 2005, 127, 2324-2333
3. Gronert, S.; Li, K. H.; Horuichi, M. “Manipulating the Fragmentation Patterns of Phosphopeptides via Gas-Phase Boron Derivatization: Determining Phosphorylation Sites in Peptides with Multiple Serines,” J. Am. Soc.Mass Spectrom. 2005, 16, 1905-1914.
4. Gronert, S. “An Alternative Interpretation of the C-H Bond Strengths in Alkanes,” J. Org. Chem. 2006, 71, 1209-1219.
5. Temple, A.; Yen, T.-Y.; Gronert, S. “Identification of Specific Protein Carbonylation Sites in Model Oxidations of Human Serum Albumin,” J. Am. Soc. Mass Spectrom. 2006, 17, 1172-1180.
6. Gronert, S.; Keeffe, J. “Primary Semiclassical Kinetic Hydrogen Isotope Effects in Identity Carbon-to-Carbon Proton- and Hydride-Transfer Reactions, an ab Initio and DFT Computational Study,” J. Org. Chem. 2006, in press.
7. Gronert, S. “Evidence that Alkyl Substitution Provides Little Stabilization to Radicals: The C-C Bond Test and the Non-Bonded Interaction Contradiction,” J. Org. Chem. 2006, in press.

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