Research Interests

I received my Ph.D. doing physical chemistry, spent a postdoctoral year learning some biochemistry, and have wandered between the two poles ever since, with the 'centroid' in Bioinorganic Chemistry. One major component of our work has been the development of electron-nuclear double resonance into a precise and incisive tool for the study of metalloenzyme active sites. Our recent studies of catalytic intermediates that form during the activation of dioxygen by heme enzymes (eg. P450; heme oxygenase) and during the reduction of dinitrogen by nitrogenase have been exceptionally informative. In the latter case, although a complicated kinetic scheme has been in hand for almost thirty years, my collaborators and I have only recently made the first connection between a 'black box' in a kinetic scheme and a characterizable trapped intermediate. A second thread to our research has been the study of inter-protein electron transfer. Here we have come to recognize that the transfer of an electron across a dynamic protein-protein interface almost invariably is controlled not by the ET process itself, but by the dynamics of conformational conversion at the interface. In the 'background', I've managed to study molecular metals and to collaborate in developing the chemistry of porphyrazine macrocycles for materials and biomedical applications.

Membership Type


Election Year


Primary Section

Section 14: Chemistry

Secondary Section

Section 29: Biophysics and Computational Biology