| NSF Org: |
CHE Division Of Chemistry |
| Recipient: |
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| Initial Amendment Date: | April 15, 2010 |
| Latest Amendment Date: | March 21, 2012 |
| Award Number: | 0951999 |
| Award Instrument: | Continuing Grant |
| Program Manager: |
Colby Foss
cfoss@nsf.gov (703)292-5327 CHE Division Of Chemistry MPS Directorate for Mathematical and Physical Sciences |
| Start Date: | April 15, 2010 |
| End Date: | March 31, 2014 (Estimated) |
| Total Intended Award Amount: | $259,000.00 |
| Total Awarded Amount to Date: | $259,000.00 |
| Funds Obligated to Date: |
FY 2011 = $80,000.00 FY 2012 = $80,000.00 |
| History of Investigator: |
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| Recipient Sponsored Research Office: |
345 BOYER AVE WALLA WALLA WA US 99362-2067 (509)527-5990 |
| Sponsor Congressional District: |
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| Primary Place of Performance: |
345 BOYER AVE WALLA WALLA WA US 99362-2067 |
| Primary Place of
Performance Congressional District: |
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| Unique Entity Identifier (UEI): |
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| Parent UEI: |
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| NSF Program(s): |
Molecular Biophysics, Chemistry of Life Processes |
| Primary Program Source: |
01001112DB NSF RESEARCH & RELATED ACTIVIT 01001213DB NSF RESEARCH & RELATED ACTIVIT |
| Program Reference Code(s): |
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| Program Element Code(s): |
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| Award Agency Code: | 4900 |
| Fund Agency Code: | 4900 |
| Assistance Listing Number(s): | 47.049 |
ABSTRACT
This award in the Chemistry of Life Processes (CLP) program, co-funded with the Division of Molecular and Cellular Biosciences (MCB), supports work by Professor Tim Machonkin at Whitman College to understand the fundamental determinants of how certain enzymes bind and carry out chemical transformations on chlorinated hydroquinones. Some bacteria have the remarkable ability to break down stable aromatic compounds, including in rare cases chlorinated aromatics. Certain types of iron-containing enzymes are involved in these processes. Among the least studied are ones that specifically recognize and cleave chlorinated hydroquinones. These hydroquinone dioxygenases appear to have evolved recently to degrade synthetic compounds that entered the environment from human activity. The factors that determine how these enzymes specifically recognize and carry out the ring-cleaving reaction on chlorinated hydroquinones are unknown. Thus, hydroquinone dioxygenases provide an ideal platform for learning how proteins can specifically bind chlorinated molecules and activate them for chemical transformations, as well as how metalloenzymes (such as iron-containing ring-cleaving enzymes) evolve new functions.
This work will immerse a significant number of undergraduate students in cutting-edge biochemical research involving an array of techniques, promoting the integration of teaching and research at this primarily undergraduate institution. The knowledge gained from this research could be applied to other classes of iron-containing enzymes involved the breakdown of aromatic molecules, and could lead to engineering of enzymes with novel properties. This, in turn, could lead to improved methods for bioremediation of chlorinated aromatic molecules, which are common intractable environmental pollutants.
PUBLICATIONS PRODUCED AS A RESULT OF THIS RESEARCH
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PROJECT OUTCOMES REPORT
Disclaimer
This Project Outcomes Report for the General Public is displayed verbatim as submitted by the Principal Investigator (PI) for this award. Any opinions, findings, and conclusions or recommendations expressed in this Report are those of the PI and do not necessarily reflect the views of the National Science Foundation; NSF has not approved or endorsed its content.
Many intractable pollutants in the environment are chlorinated compounds. Certain soil bacteria have been identified that can degrade a few of these compounds and are therefore of interest for use in bioremediation; however, little is known about the enzymes involved. Our research has focused on one enzyme from such a bacterium, and has demonstrated that it is indeed specific for chlorinated over non-chlorinated compounds. We have begun to explore the origin of this unusual substrate specificity. One possible mechanism is a weak interaction between the chlorine atom of the substrate and the iron ion located at the enzyme active site. Through the use of synthetic model compounds, we have characterized the nature of this little-studied type of interaction and the role it could play in the determining the enzyme’s unique specificity.
This research was performed by undergraduate students (12 total over the course of four years), working at Whitman College, at the lab of a collaborator at the University of Rochester, and with me at the University of British Columbia during my sabbatical. These students participated in the research at every step of the way: reading the scientific literature, designing and executing the experiments, analyzing the data, presenting the results at regional and national meetings, and writing up the results for publication. These research experiences have had a large impact on the intellectual growth and the scientific training of these undergraduate students. Many of them have chosen to pursue careers in science: six students are either in Chemistry or Bioscience PhD programs or are starting in the Fall, and one more plans to apply. One student is teaching science through Teach for America, and the remaining students are pursuing careers in medicine. Thus, this grant had a strong positive impact on securing the “pipeline” of talented and hardworking students pursuing careers in the sciences and related areas.
Last Modified: 06/26/2014
Modified by: Timothy Machonkin
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