Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published September 1, 1990 | public
Journal Article

Organomercurial Lyase and Mercuric Ion Reductase: Nature's Mercury Detoxification Catalysts

Abstract

Concern over our increasingly polluted environment, with its potentially deleterious effects on organisms, including humans, has sparked considerable research into the strategies by which living systems contend with toxic compounds. One area of research that has been especially prolific in recent years deals with the mechanisms by which bacteria cope with increased heavy metal burdens. Heavy metals are prevalent throughout the biosphere, and while some (e.g., Co, Cu, Mo, Ni, and Zn) are required in trace amounts, elevated concentrations of most are deleterious by virtue of their avid ligation to cellular components, particularly proteins. Especially toxic to higher organisms are organometallics, whose lipophilic nature gives them a strong tendency toward bioaccumulation in the food chain.

Additional Information

© 1990 American Chemical Society. Received January 26, 1990. Revised Manuscript Received May 14, 1990. We acknowledge the significant contributions to the Mer A and Mer B projects made in this laboratory by Drs. Barbara Fox, Karin Au, Peter Schultz, Tadhg Begley, and Alan Waltz. Additionally, many of the experiments described in the Mer A section were performed in collaboration with Drs. Susan Miller, Vincent Massey, David Ballou, and Charles Williams, Jr., at the Cniuersity of Michigan; current understanding of the MerA mechanism is due in large part their input and expertise. Nikolaus Schiering and Dr. Emil Pai at the Max Planck Institut fur Medizinische Forschung, Heidelberg, FRG, continue efforts to solve the Mer A crystal structure.

Additional details

Created:
August 19, 2023
Modified:
October 18, 2023