Understanding the Biological Chemistry of Mercury Using a de novo Protein Design Strategy

Research output: Chapter in Book/Report/Conference proceedingChapter

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Abstract

Hg(II) is a well known toxin that has a high affinity for protein thiolate functional groups. While an area of significance, a dearth of literature exists on the chemistry of Hg(II) with thiolate containing proteins. In this chapter we demonstrate the design of proteins that complex Hg(II) in linear, trigonal planar, and tetrahedral environments. Physical techniques such as 199Hg NMR, 199mHg PAC and UV-vis spectroscopy to characterize Hg(II) sites in proteins are also described along with the application of our understanding of Hg(II) interactions with designed proteins to address the binding of Hg(II) in protein sites such as MerA (2-coordinate), MerR (3-coordinate) and Hg substituted rubredoxin (4-coordinate). Finally, knowledge from this system is used to predict the chemistry of Hg(II) bound forms of Hahl at high pH.
Original languageUnknown
Title of host publicationBioinorganic Chemistry: cellular systems and synthetic models
Editors Long, C. E., M. J. Baldwin
Place of PublicationWashington, DC
PublisherAmerican Chemical Society
Pages183-197
ISBN (Print)9780841269750/ 9780841224865
Publication statusPublished - 1 Jan 2009

Publication series

NameACS Symposium Series
PublisherAmerican Chemical Society
ISSN (Print)0097-6156

Cite this

Casanova, O. I. (2009). Understanding the Biological Chemistry of Mercury Using a de novo Protein Design Strategy. In Long, C. E., & M. J. Baldwin (Eds.), Bioinorganic Chemistry: cellular systems and synthetic models (pp. 183-197). (ACS Symposium Series). American Chemical Society. http://dx.doi.org/10.1021/bk-2009-1012.ch012