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Title: Metal binding proteins, recombinant host cells and methods

Patent ·
OSTI ID:1174899

The present disclosure provides artificial heavy metal binding proteins termed chelons by the inventors. These chelons bind cadmium and/or mercuric ions with relatively high affinity. Also disclosed are coding sequences, recombinant DNA molecules and recombinant host cells comprising those recombinant DNA molecules for expression of the chelon proteins. In the recombinant host cells or transgenic plants, the chelons can be used to bind heavy metals taken up from contaminated soil, groundwater or irrigation water and to concentrate and sequester those ions. Recombinant enteric bacteria can be used within the gastrointestinal tracts of animals or humans exposed to toxic metal ions such as mercury and/or cadmium, where the chelon recombinantly expressed in chosen in accordance with the ion to be rededicated. Alternatively, the chelons can be immobilized to solid supports to bind and concentrate heavy metals from a contaminated aqueous medium including biological fluids.

Research Organization:
University of Georgia Research Foundation, Inc., Athens, GA (Unites States)
Sponsoring Organization:
USDOE
DOE Contract Number:
FG02-99ER62865
Assignee:
University of Georgia Research Foundation, Inc. (Athens, GA)
Patent Number(s):
6,750,042
Application Number:
09/977,137
OSTI ID:
1174899
Country of Publication:
United States
Language:
English

References (15)

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Alternative Routes for Entry of HgX 2 into the Active Site of Mercuric Ion Reductase Depend on the Nature of the X Ligands journal March 1999
Communication between the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis journal March 1991
Transition metals in control of gene expression journal August 1993
Ultrasensitivity and heavy-metal selectivity of the allosterically modulated MerR transcription complex. journal May 1990
The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer journal February 1990
Cd(II)-Responsive and Constitutive Mutants Implicate a Novel Domain in MerR journal June 1999
Bacterial metal-resistance proteins and their use in biosensors for the detection of bioavailable heavy metals journal April 2000
Repeated fed-batch operations for microbial detoxification of mercury using wild-type and recombinant mercury-resistant bacteria journal October 1998
A Fluorescent Zinc Probe Based on Metal-Induced Peptide Folding journal January 1996
Construction of a synthetic gene for the metalloregulatory protein MerR and analysis of regionally mutated proteins for transcriptional regulation journal April 1994
C-Terminal cysteines of Tn501 mercuric ion reductase journal February 1992

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