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My research program focuses the reaction mechanisms of oxidoreductase enzymes - particularly those possessing molybdenum or flavin in their active sites - and biological electron transfer. The molybdenum-containing enzymes catalyze the incorporation of oxygen into a variety of organic and inorganic compounds, and constitute an important enzyme class within the oxidoreductases. These enzymes have been only poorly understood in comparison to other biological systems that contain heme, flavin, non-heme iron or copper. Working with representative members of each of the three major families of molybdenum enzymes, we have successfully identified the fundamental aspects of the catalytic sequences of these enzymes, and in each case established the overall chemical course of the reaction. Particularly in the case of the molybdenum hydroxylase family (as represented by xanthine oxidase), work in our laboratory has elucidated the overall reaction mechanism, characterizing each of the principal intermediates in the course of the reaction both spectroscopically and crystallographically. Current work focuses on two ancient yet poorly understood enzymes, formate dehydrogenase and CO dehydrogenase.
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Journal of Biological Chemistrypp.107524-107524, (2024)
BIOCHEMISTRYno. 24 (2023): 3554-3567
The Journal of biological chemistryno. 9 (2023): 105189-105189
Methods in enzymology (2023): 531-550
The Journal of biological chemistryno. 7 (2023): 104853-104853
Journal of the American Chemical Societyno. 47 (2023): 25850-25863
Journal of Biological Chemistryno. 3 (2023): 103676-S352
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