J. Hugh McDowell, Ph.D.

Dr. McDowellAcademic Title


Contact Information

(352) 273-8789 (phone)




Dr. McDowell began his work on the biochemistry and biophysics of vision when he began graduate school in 1969. He received his Ph.D. degree from the Molecular Biophysics program at Florida State University in 1974. He continued his study of the biochemistry of vision when he studied the phosphorylation of rhodopsin during 2 years of postdoctoral work with Dr. Hermann Kühn at the Kerforschungsanlage, Jülich, Germany.

Dr. McDowell then joined the laboratory of Dr. Paul Hargrave first as a postdoctoral fellow and then as research faculty at Southern Illinois University, Carbondale, Illinois. With Dr. Hargrave, he worked on the primary structure of rhodopsin as well as the topography of the rhodopsin molecule as it sits in the membrane of the rod cells. He moved with Dr. Hargrave to the University of Florida’s Department of Ophthalmology in 1985. Using protein and peptide chemistry techniques as well as various biophysical and biochemical techniques he has continued to explore the activation and de-activation of the visual process.

Dr. W. Clay Smith joined the laboratory bringing molecular biology expertise to the group and then developed his own research group studying arrestin’s functions in the visual system as well as other aspects of the visual processes. Dr. McDowell worked with both Dr. Hargrave and Dr. Smith and on Dr. Hargrave’s retirement, joined Dr. Smith’s research group where he continues studies of the biochemistry and biophysics of visual processes.


  • McDowell, J.H., H. Kühn. 1977. Light-induced phosphorylation of rhodopsin in cattle photoreceptor membranes: substrate activation and inactivation. Biochemistry. 16: 4054-60
  • Hargrave, P.A., J.H. McDowell, D.R. Curtis, J.K. Wang, E. Juszczak, S.-L. Fong, J.K. Rao, P. Argos. 1983. The structure of bovine rhodopsin. Biophys. Struct. Mech. 9: 235-44
  • J.H. McDowell, W.C. Smith, R.L. Miller, M. Popp, A. Arendt, G. Abdulaeva, and P.A. Hargrave “Sulfhydryl Reactivity Demonstrates Different Conformational States for Arrestin, Arrestin Activated by a Synthetic Phosphopeptide, and Constitutively Active Arrestin” Biochenistry 38, 6119-6125 (1999)
  • J.H. McDowell, P.R. Robinson, R.L. Miller, M.T.Bannock, A. Arendt, W.C. Smith, and P.A. Hargrave. “Activation of Arrestin: Requirement of Phosphorylation as the Negative Charge on residues in Synthetic Peptides from the Carboxyl-Terminal Region of Rhodopsin”, Invest. Ophthalmol. Vis. Sci. 42, 1439-1443 (2001)
  • J. J. Peterson, B. M. Tam, O. L. Moritz, C. L. Shelamer, D. R. Dugger, J. H. McDowell, P. A. Hargrave, D. S. Papermaster, W. C. Smith. Arrestin Migrates in Photoreceptors in Response to Light: a Study of Arrestin Localization Using an Arrestin-GFP Fusion Protein in Transgenic Frogs. Experimental Eye Research 76, 553-563 (2003)
  • W. Clay Smith1,2, Susan Bolch1, Donald R. Dugger1, Jian Li1, Isi Esquenazi1, Anatol Arendt1, Del Benzenhafer1, J. Hugh McDowell1. Interaction Of Arrestin With Enolase1 In Rod Photoreceptors. Submitted for publication, 2010