Phil Huskey

Associate Professor

Research Interests
Representative Publications

Some Recent Courses

Organic Chemistry I
Chemical Kinetics and Mechanism
Organic Chemistry II
Physical Chemistry I

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Phil Huskey Associate Professor email: huskey@rutgers.edu phone: 973-353-5741

Research Interests

A central theme in our research is the study of the origins of the catalytic power and dynamic behavior of enzymes. Our projects can be classified according to the following areas:

(1) Energetics of reactions catalyzed by enzymes: In recent years it has been learned that the rate of many enzyme-catalyzed reactions is controlled not by a single rate-limiting mechanistic step, but by multiple rate-limiting steps. We are using kinetic isotope effects to learn about the free-energy profiles of these complex enzymatic reactions. Ultimately our work should contribute to knowledge about the evolution of enzyme function and the origins of catalytic power.

(2) Enzyme kinetics under conditions open to the flow of mass: Conventional studies of enzymatic reactions are conducted under batch conditions where there is no flow of mass into the experimental system. Because biological systems are in fact open to mass flow, it is suspected new insights into the function of enzymes can be obtained from experiments conducted under flow conditions, open to mass.

(3) Vibrational modeling of transition-states: To aid our interpretations of kinetic isotope effects, computational approaches to modeling the vibrations of transition states are used.

Representative Publications

• Transition-State Responses to Amino-Acid Perturbations in Yeast Pyruvate Decarboxylase: A Carbon Isotope Effect Study. L. Chen, Y. Yuan, and W. P. Huskey J. Phys. Org. Chem. 2004, 17, 572-578.

• Enzymatic Reaction of Silent Substrates: Kinetic Theory and Application to the Serine Protease Chymotrypsin. A. Case, W. P. Huskey, and R. L. Stein Biochemistry, 2003, 4727-4732.

• Hydrogen Bonding to Active-Site Histidine in Peptidyl Boronic Acid Inhibitor Complexes of Chymotrypsin and Subtilisin: Proton Magnetic Resonance Assignments and H/D Fractionation. Catalysis by Thiamin-Dependent Enzymes. D. Bao, W. P. Huskey, C. A. Kettner, and F. Jordan J. Am. Chem. Soc. 1999, 121, 4684-4689.

• Carbon Isotope Effects on kcat for Formate Dehydrogenase Determined Unsing a Continuous-Flow Stirred-Tank Reactor. H. Xue, X. Wu, and W. P. Huskey J. Am. Chem. Soc. 1996, 118, 5804-5805.

• Model Calculations of Isotope Effects Using Structures Containing Low-Barrier Hydrogen Bonds. W. P. Huskey J. Am. Chem. Soc. 1996, 118, 1663-1668.