Education and Training
B.S., Baylor University, Waco, Texas
Ph.D., California Institute of Technology, Pasadena, California
Before coming to Rensselaer Polytechnic Institute in 2004, Dr. Morgan worked in the laboratory of Prof. Mårten Wikström at the University of Helsinki (Helsinki, Finland) and in the laboratory of Prof. Robert Gennis at the University of Illinois at Urbana-Champaign (Urbana, Illinois).
Tel: (518) 276-4170
Fax: (518) 276-2851
Office: Biotechnology Center Rm. 2137
Rensselaer Polytechnic Institute
110 8th Street
Troy, NY 12180-3596
Energy production in biological systems (Bioenergetics), cellular respiration, photosynthesis, heme-copper oxidases, bacteriorhodopsin, rapid enzyme kinetics measured by visible, electrometric and Fourier-tranform infrared.
Dr. Morgan is interested in energy transduction in biological systems. Living organisms require a constant supply of energy. In the cells themselves, this energy must be available in the form of ATP, but organisms obtain energy from their environment in other, very different forms, such as oxygen, carbohydrates, light, etc. This means that living organisms must be able to efficiently convert energy into forms which are useable in the cell. The goal of this research is to understand how this energy conversion takes place—a description in terms of physics and chemistry.
This problem requires an interdisciplinary approach, but the central experimental methods of interest are microsecond time-resolved spectroscopy and kinetics. An important current challenge is to apply the methods of time-resolved infrared spectroscopy (FTIR) to enzyme systems that cannot be repeatedly cycled by light. Dr Morgan and collaborators are approaching this problem by bringing together microfluidic sample handling and time resolved FTIR spectroscopy.
Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen. Jasaitis, A., Verkhovsky, M. I., Morgan, J. E., and Wikström, M. (1999) Biochemistry, 38, 2697-2706.
Role of the PR intermediate in the reaction of cytochrome c oxidase with O2. Morgan, J. E., Verkhovsky, M. I., Palmer, G., and Wikström, M. (2001) Biochemistry, 40, 6882-92.
A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides results in an increase in steady-state activity but completely eliminates proton pumping. Pawate, A.S., Morgan, J., Namslauer, A., Mills, D., Brzezinski, P., Ferguson-Miller S., and Gennis, R. B. (2002) Biochemistry, 41, 13417-23.
Replacing Asn207 by aspartate at the neck of the D channel in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides results in decoupling the proton pump, Han, D., Namslauer, A., Pawate, A., Morgan, J. E., Nagy, S., Vakkasoglu A. S., Brzezinsku, P. and Gennis, R. B. (2006) Biochemistry, 45, 14064-74.
Microfluidic flow-flash: method for investigating protein dynamics, Toepke, M. W., Brewer, S. H., Vu, D. M., Rector, K. D., Morgan, J. E., Gennis, R. B., Kenis, P. J., and Dyer, R. B., (2007) Anal. Chem. 79, 122-8.
Water structural changes in the L and M photocycle intermediates of bacteriorhodopsin as revealed by time-resolved step-scan Fourier transform infrared (FTIR) spectroscopy, Morgan, J. E., Vakkasoglu, A. S., Gennis, R. B., and Maeda, A. (2007) Biochemistry