Pyranopterin Coordination Controls Molybdenum Electrochemistry in Escherichia coli Nitrate Reductase
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Abstract
Molybdenum is an essential trace element for most species on the earth. Molybdoenzymes (enzymes containing Molybdenum) play diverse roles in human health, global geochemical cycles, and bacterial metabolism. Interestingly, nitrate reductase (NarGHI) isolated from the common gut bacterium Escherichia coli is an ideal model to study how Mo functions. Molybdenum does not act alone but is held in molybdoenzymes by a complex organic molecule called molybdenum cofactor. I studied the molybdenum cofactor in NarGHI. My research addressed the role of amino acids in the protein that interact with the molybdenum cofactor and the result suggested that the organic component of the cofactor plays a pivotal role in controlling enzyme activity. This research offers a broad implication in the field of molybdoenzyme research and can potentially benefit drug development for molybdoenzyme-related diseases.