A Caltech Library Service

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

Moore, Melissa J. and Distefano, Mark D. and Zydowsky, Lynne D. and Cummings, Richard T. and Walsh, Christopher T. (1990) Organomercurial Lyase and Mercuric Ion Reductase: Nature's Mercury Detoxification Catalysts. Accounts of Chemical Research, 23 (9). pp. 301-308. ISSN 0001-4842. doi:10.1021/ar00177a006.

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item:


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.

Item Type:Article
Related URLs:
URLURL TypeDescription
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.
Funding AgencyGrant Number
NSF Predoctoral FellowshipUNSPECIFIED
Helen Hay Whitney FoundationUNSPECIFIED
Damon Runyon-Walter Winchell Cancer FundUNSPECIFIED
NIH Postdoctoral FellowshipUNSPECIFIED
Issue or Number:9
Record Number:CaltechAUTHORS:20180315-075026014
Persistent URL:
Official Citation:Organomercurial lyase and mercuric ion reductase: nature's mercury detoxification catalysts Melissa J. Moore, Mark D. Distefano, Lynne D. Zydowsky, Richard T. Cummings, and Christopher T. Walsh Accounts of Chemical Research 1990 23 (9), 301-308 DOI: 10.1021/ar00177a006
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:85323
Deposited By: Ruth Sustaita
Deposited On:16 Mar 2018 15:36
Last Modified:15 Nov 2021 20:27

Repository Staff Only: item control page