This research project concerns the study of enzyme reaction mechanisms, protein structure-function relationships, protein-protein interactions, protein biosynthesis, and mechanisms of long range biological electron transfer. The results of these studies are helping us to understand mechanisms by which enzymes catalyze reactions, and the molecular details of biological energy transduction and respiration. The proposed studies focus on the tryptophan tryptophylquinone [TTQ] bearing enzyme, methylamine dehydrogenase [MADH], and the electron transfer complex it forms with the type I copper protein amicyanin, and cytochrome c-551i . The proteins in this project have been crystallized free and in complex, and protocols have been established for altering the proteins by site-directed mutagenesis and analyzing their physical properties and physiological functions. This allows us define specific structure-function relationships. Elucidation of factors which influence the specific protein-protein interactions that are required for efficient interprotein electron transfer is providing insight into the process of protein-protein recognition that is common to a wide range of biologic phenomena. Characterization of the catalytic reaction mechanisms of quinoproteins is allowing us to better understand how enzymes, in general, catalyze reactions. Definition of the mechanisms of long range intermolecular electron transfer will allow us to better understand the fundamental processes of respiration and intermediary metabolism at the molecular level. Description of the mechanism of biosynthesis of MADH and TTQ will be relevant to understanding the mechanisms of biosynthesis of complex redox proteins, as well as mechanisms of protein biosynthesis and posttranslational modification of proteins in general.
Showing the most recent 10 out of 145 publications
