This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. We propose to use X-ray absorption spectroscopy to study the molecular mechanisms of heavy metal detoxification by the bacterial mercury resistance system, encoded by the Tn501 mer operon. The mer system employs metal transport proteins, enzymes for transformation and reduction of mercury species to elemental volatile Hg(0), and a paradigmatic metalloregulatory system (based on MerR), all of which demonstrate specificity for Hg. In general, we are interested in elucidating the molecular mechanisms involved and in investigating the potential for engineering this system to handle other heavy metals (Cd, Au, etc.) for bioremediation. This particular program has two major targets: (a) MerR, its interactions with merO/P and/or RNA polymerase, and the role of MerD which appears to be involved in relieving MerR activation;(b) MerA (mercuric reductase) and variants that have now been shown to also catalyze the reduction of Au(III) to Au(I), with eventual disproportionation to form Au(0) colloids.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-30
Application #
7954354
Study Section
Special Emphasis Panel (ZRG1-BPC-E (40))
Project Start
2009-03-01
Project End
2010-02-28
Budget Start
2009-03-01
Budget End
2010-02-28
Support Year
30
Fiscal Year
2009
Total Cost
$3,302
Indirect Cost
Name
Stanford University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
009214214
City
Stanford
State
CA
Country
United States
Zip Code
94305
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