Crystal structures of the organomercurial lyase MerB in its free and mercury-bound forms: insights into the mechanism of methylmercury degradation.

Abstract

Bacteria resistant to methylmercury utilize two enzymes (MerA and MerB) to degrade methylmercury to the less toxic elemental mercury. The crucial step is the cleavage of the carbon-mercury bond of methylmercury by the organomercurial lyase (MerB). In this study, we determined high resolution crystal structures of MerB in both the free (1.76-A resolution… (More)
DOI: 10.1074/jbc.M807143200

Cite this paper

@article{LafranceVanasse2009CrystalSO, title={Crystal structures of the organomercurial lyase MerB in its free and mercury-bound forms: insights into the mechanism of methylmercury degradation.}, author={Julien Lafrance-Vanasse and Maryse Lefebvre and Paola Di Lello and Jurgen Sygusch and James G Omichinski}, journal={The Journal of biological chemistry}, year={2009}, volume={284 2}, pages={938-44} }