Some microbes can metabolize inorganic and organic mercury to less toxic forms using the MerR protein. Using small-angle X-ray scattering (SAXS) complemented by molecular dynamics simulations, a scientific team from the Universities of Tennessee, Georgia and California at San Francisco and Oak Ridge National Laboratory determined that when a single mercury ion binds to the MerR protein a structural change is induced. This structural change turns on the DNA transcription machinery for several other proteins and enzymes involved in removing the toxic mercury from the cell. Understanding the mechanism by which the proteins in these microorganisms bind to and metabolize mercury could be useful for identifying biological strategies for removing or transforming mercury in groundwater or soils.
Reference: Guo, H-B., A. Johs, J.M. Parks, L. Olliff, S.M. Miller, A.O. Summers, L. Liang and J.C. Smith. 2010. "Structure and Conformational Dynamics of the Metalloregulator MerR upon Binding of Hg(II)." Journal of Molecular Biology 398: 555-568.
Contact: Paul E. Bayer, SC-23.1, (301) 903-5324
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