Molecular Sciences, School of Bioenergy and Photosynthesis,
Arizona State University
United States of America
James P. Allen is a Professor of Molecular Sciences at Arizona State University. For his PhD degree from the University of Illinois at Urbana-Champaign, Professor James Allen used electron paramagnetic resonances to examine the biophysical properties of proteins in terms of their fractal behavior. As a postdoctoral fellow in the group of Professor George Feher at the University of California, San Diego, he began his ongoing studies on energy transduction processes in photosynthesis. While at UCSD, he examined the ability of a pigment-protein complex known as the bacterial reaction center to perform the primary processes in photosynthesis, the conversion of light energy into a charge-separated state. As part of these studies, he was part of a group that pioneered structural studies of membrane proteins as they determined three-dimensional structure of the bacterial reaction center. This experience has evolved to his current research interests in biophysics and biochemistry with a focus on the role of proteins in energy and disease.
In the broadest sense, our research objectives are to understand how proteins function in biological systems. Our interests range from understanding how energy is converted in photosynthetic systems to how changes in proteins can cause certain diseases. We use a variety of biochemical and biophysical approaches to examine each problem, with an emphasis on relating the functional properties to the structure. Therefore, one major aspect of our research is the determination of the three-dimensional structures of proteins by x-ray crystallography. The structural studies are complemented with various spectroscopic measurements of the proteins with modifications of certain amino acid residues. One major focus is the photosynthetic process, the conversion of light energy into chemical energy that involves a variety of pigment-protein complexes. Our research goal is to develop models for the transfer of electrons and energy in these complexes, in particular to understand how these processes changed as primitive bacteria evolved into cyanobacteria and plants. To achieve this goal, we create bacterial complexes with new Mn cofactors that resembles the site of water oxidation in cyanobacteria and plants. In addition, we apply the concepts learned from the natural systems to artificial systems with the goal of re-creating specific functional aspects. For example, we design artificial proteins with Mn cofactors and compare their properties, including the ability to catalyze redox reactions, with Mn-binding proteins found in nature.
"Copper environment in artificial metalloproteins probed by electron paramagnetic spectroscopy," M. Flores, T. L. Olson, D. Wang, S. Edwardraja, S. Shinde, G. Ghirlanda, J. C. Williams, and J. P. Allen , Journal of Physical Chemistry B 119 13825-13833 (2015)
"The SMN structure reveals its crucial role in snRNP assembly," C. O. Seng, C. Magee, C. Lorson, and J. P. Allen , Hum. Mol. Genet. (2015)
"Identification of amino acids at the catalytic site of a ferredoxin-dependent cyanobacterial nitrate reductase," A. P. Srivastava, J. P. Allen, B. J. Vaccaro, M. K. Johnson, M. Hirasawa, S. Alkul, and D. B. Knaff , Biochemistry 54 5557-5568 (2015)