Team:Groningen/Project/Accumulation

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===Metallothioneins===
===Metallothioneins===
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Metallothioneins are a class of low molecular-weight metal-binding proteins rich in cysteines residues. They are capable of binding a variety of heavy metals including Hg<SUP><FONT SIZE="-1">2+</FONT></SUP>. And they have readily been used to create cell based systems for purification of contaminated water <SUP><FONT SIZE="-1">[http://www.ncbi.nlm.nih.gov/pubmed/9758654][http://www.ncbi.nlm.nih.gov/pubmed/18618649]</FONT></SUP>.
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Metallothioneins are a class of low molecular-weight metal-binding proteins rich in cysteines residues. They are capable of binding a variety of heavy metals including Hg<SUP><FONT SIZE="-1">2+</FONT></SUP>. And they have readily been used to create cell based systems for purification of contaminated water <SUP><FONT SIZE="-1">[http://www.ncbi.nlm.nih.gov/pubmed/9758654][http://www.ncbi.nlm.nih.gov/pubmed/18618649]</FONT></SUP>. In addition to their wide application possibilities they also have the capacity to carry multiple metal ions at one time, in contrast to other metalloproteins that carry them one-on-one<SUP><FONT SIZE="-1">[http://www.ncbi.nlm.nih.gov/pubmed/9579658]</FONT></SUP>.
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Many forms of metallothioneins are known and their affinity for different metals has been investigated on several occasions, such as for cadmium<SUP><FONT SIZE="-1">[http://www.ncbi.nlm.nih.gov/pubmed/16890348]</FONT></SUP>, arsenic <SUP><FONT SIZE="-1">[http://www.ncbi.nlm.nih.gov/pubmed/16984198]</FONT></SUP>, mercury<SUP><FONT SIZE="-1">[[http://www.ncbi.nlm.nih.gov/pubmed/9758654 1]][http://www.ncbi.nlm.nih.gov/pubmed/9342882][http://www.ncbi.nlm.nih.gov/pubmed/17920767]</FONT></SUP>, nickel <SUP><FONT SIZE="-1">[http://www.ncbi.nlm.nih.gov/pubmed/12727263]</FONT></SUP> or a combination of metals<SUP><FONT SIZE="-1">[[http://www.ncbi.nlm.nih.gov/pubmed/9579658 3]][http://www.ncbi.nlm.nih.gov/pubmed/18313216]</FONT></SUP>.
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===Alternatives===
===Alternatives===
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{{todo|(Bacterio)Ferritins}}<br>
{{todo|(Bacterio)Ferritins}}<br>
{{todo|Phytochelatins}}
{{todo|Phytochelatins}}
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 +
===Inhibitory characteristics?===
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 +
===Requirements===
==Literature==
==Literature==
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#Chen <i>et al.</i>: [http://www.ncbi.nlm.nih.gov/pubmed/9758654 Hg<SUP><FONT SIZE="-1">2+</FONT></SUP> removal by genetically engineered Escherichia coli in a hollow fiber bioreactor], Biotechnology progress 1998;14(5)667-71
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#Chen <i>et al.</i>: [http://www.ncbi.nlm.nih.gov/pubmed/9758654 Hg<SUP><FONT SIZE="-1">2+</FONT></SUP> removal by genetically engineered Escherichia coli in a hollow fiber bioreactor], Biotechnology progress (1998) 14(5);667-71
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#{{todo|Brady <i>et al.</i>:[http://www.ncbi.nlm.nih.gov/pubmed/18618649 The use of hollow fiber cross-flow microfiltration in bioaccumulation and continuous removal of heavy metals from solution by <i>Saccharomyces cerevisiae</i>], Biotechnology and bioengineering 1994;44(11):1362-6}}
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#{{todo|Brady <i>et al.</i>:[http://www.ncbi.nlm.nih.gov/pubmed/18618649 The use of hollow fiber cross-flow microfiltration in bioaccumulation and continuous removal of heavy metals from solution by <i>Saccharomyces cerevisiae</i>], Biotechnology and bioengineering (1994) 44(11);1362-1366}}
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#Fowler: [http://www.ncbi.nlm.nih.gov/pubmed/3297654 Intracellular Compartmentation of Metals in Aquatic Organisms: Roles in Mechanisms of Cell injury], Environmental Health Perspectives 1987;71 121-128
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#<b>Chang <i>et al.</i>:[http://www.ncbi.nlm.nih.gov/pubmed/9579658 Cysteine contributions to metal binding preference for Zn/Cd in the b-domain of metallothionein], Protein Engineering 1998 11(1);41–46</b>
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#Deng <i>et al.</i>:[http://www.ncbi.nlm.nih.gov/pubmed/16890348 Cadmium removal from aqueous solution by gene-modified Escherichia coli JM109] Journal of hazardous materials (2007) 139(2);340-4
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#Ngu & Stillman: [http://www.ncbi.nlm.nih.gov/pubmed/16984198 Arsenic binding to human metallothionein], Journal of the American Chemical Society (2006) 128(38);12473-83.
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#Chen & Wilson: [http://www.ncbi.nlm.nih.gov/pubmed/9342882 Genetic engineering of bacteria and their potential for Hg<SUP><FONT SIZE="-1">2+</FONT></SUP>  bioremediation], Biodegradation (1997) 8(2);97-103
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#Deng <i>et al.</i>: [http://www.ncbi.nlm.nih.gov/pubmed/17920767 Continuous treatment process of mercury removal from aqueous solution by growing recombinant E. coli cells and modeling study], Journal of hazardous materials (2008) 153(1-2);487-92
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#Deng <i>et al.</i>: [http://www.ncbi.nlm.nih.gov/pubmed/12727263 Bioaccumulation of nickel from aqueous solutions by genetically engineered Escherichia coli], Water research (2003) 37(10);2505-11.
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#Kao <i>et al.</i>: [http://www.ncbi.nlm.nih.gov/pubmed/18313216 Biosorption of nickel, chromium and zinc by MerP-expressing recombinant Escherichia coli], Journal of hazardous materials (2008) 158(1);100-106
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#Fowler: [http://www.ncbi.nlm.nih.gov/pubmed/3297654 Intracellular Compartmentation of Metals in Aquatic Organisms: Roles in Mechanisms of Cell injury], Environmental Health Perspectives (1987) 71;121-128

Revision as of 18:09, 7 June 2009

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Introduction

Once heavy metals have entered the cell it is key to keep them there. As these metals are toxic to cell survival in critical amounts evolution has provided us with biological detoxicification proteins such as metallothioneins. These proteins can aid us in our quest to accumulate a variaty of heavy metals as they bind to a wide range of metals including cadmium, zinc, mercury, copper, arsenic, silver, etc..

Metallothioneins

Metallothioneins are a class of low molecular-weight metal-binding proteins rich in cysteines residues. They are capable of binding a variety of heavy metals including Hg2+. And they have readily been used to create cell based systems for purification of contaminated water [2][3]. In addition to their wide application possibilities they also have the capacity to carry multiple metal ions at one time, in contrast to other metalloproteins that carry them one-on-one[4]. Many forms of metallothioneins are known and their affinity for different metals has been investigated on several occasions, such as for cadmium[5], arsenic [6], mercury[1][7][8], nickel [9] or a combination of metals[3][10].


Alternatives

Inclusion bodies[11]
(Bacterio)Ferritins
Phytochelatins

Inhibitory characteristics?

Requirements

Literature

  1. Chen et al.: Hg2+ removal by genetically engineered Escherichia coli in a hollow fiber bioreactor, Biotechnology progress (1998) 14(5);667-71
  2. Brady et al.:The use of hollow fiber cross-flow microfiltration in bioaccumulation and continuous removal of heavy metals from solution by Saccharomyces cerevisiae, Biotechnology and bioengineering (1994) 44(11);1362-1366
  3. Chang et al.:Cysteine contributions to metal binding preference for Zn/Cd in the b-domain of metallothionein, Protein Engineering 1998 11(1);41–46
  4. Deng et al.:Cadmium removal from aqueous solution by gene-modified Escherichia coli JM109 Journal of hazardous materials (2007) 139(2);340-4
  5. Ngu & Stillman: Arsenic binding to human metallothionein, Journal of the American Chemical Society (2006) 128(38);12473-83.
  6. Chen & Wilson: Genetic engineering of bacteria and their potential for Hg2+ bioremediation, Biodegradation (1997) 8(2);97-103
  7. Deng et al.: Continuous treatment process of mercury removal from aqueous solution by growing recombinant E. coli cells and modeling study, Journal of hazardous materials (2008) 153(1-2);487-92
  8. Deng et al.: Bioaccumulation of nickel from aqueous solutions by genetically engineered Escherichia coli, Water research (2003) 37(10);2505-11.
  9. Kao et al.: Biosorption of nickel, chromium and zinc by MerP-expressing recombinant Escherichia coli, Journal of hazardous materials (2008) 158(1);100-106
  10. Fowler: Intracellular Compartmentation of Metals in Aquatic Organisms: Roles in Mechanisms of Cell injury, Environmental Health Perspectives (1987) 71;121-128