Professor Emeritus

Office: Urey Hall Addn 3050G
Phone: 858-534-3199
Email: dmagde@ucsd.edu
Group: View group members

1972-1974

Research Associate, Washington State University

1970-1972

Postdoctoral Fellow, Cornell

Transition metals are often used in the active site of proteins. Premier examples include the heme (iron porphyrin) proteins.

Hemoglobin is the best known heme protein. For a decade we, and others, have built upon that prior knowledge of basic biological function and chemical characterization to unravel in ever-increasing detail exactly what features of the protein control the interaction of the iron atom with small ligands. We use fast kinetic studies with nanosecond, picosecond, and now femtosecond lasers. The accompanying graph illustrates absorption spectra recorded at one picosecond intervals.

Our recent studies now involve other heme proteins, in particular those recently recognized as important in the many processes regulated by nitric oxide, specifically nitric oxide synthase and guanylate cyclase. In addition, we have broadened out interests to include biological systems that utilize cobalt chemistry, namely vitamin B12 and its relatives. This has led to a patentable drug invention.

Perhaps fortuitously, the model compounds have also turned out to be useful for studies of fundamental aspects of chemical reactivity in a liquid environment. This has now evolved past the stage of basic characterization into a new era in which we are pioneering the use of ultrafast laser kinetic measurements in conjunction with high-pressure to change liquid density at constant temperature and composition.

Bioinorganic
Biophysics