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Research Interests
Research Interests by Gerald D. Watt.
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I am interested in the structure, function, and mechanism of catalysis
conducted by metalloenzymes such as nitrogenase, hydrogenase, and other
biological systems that contain unusual metal atoms (molybdenum,
tungsten, vanadium, etc.) or metal cluster systems. Many important
biological reactions and cycles are carried out by enzymes with unusual
metal redox clusters. Biological nitrogen reduction is the process that
involves the conversion of atmospheric dinitrogen (N2) into ammonia,
which is then used in the synthesis of biomolecules. This important
process is catalyzed by the nitrogenase enzyme, which contains the
following complex metal clusters, called FeMoco and P clusters,
responsible for dinitrogen activation and reduction.
 These metal clusters are unique to nitrogenase, although similar but nonfunctional clusters have recently been synthesized in an attempt to model the nitrogenase activity. Our interest is in examining the redox, magnetic, and spectroscopic properties as well as the chemical reactivity of these clusters in their naturally occurring protein environments. Additional studies focus on these metal clusters isolated from their protein environments in organic solvents. Metal storage proteins is another area of interest being actively investigated. The ferritins are hollow, multisubunit iron storage proteins used to provide and control the iron essential for all living systems. The assembled ferritin and a subunit are shown below. We are interested in the step-by-step events that deposit iron within the hollow interior of the ferritin molecules and those events involved in iron release when required by cellular demand. Biochemical, inorganic, and physical chemical approaches and techniques are used in these investigations.
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