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Copper clean-up idea

8741 Views 40 Replies 13 Participants Last post by  Buzz_Hog
I was gonna post this as a reply to the invert killer thread, but I though I would just start a new thread and get some ideas:

There has been a running theme of Cu contamination around here lately. Has anyone ever read about treating a tank with EDTA or some other metal-chelating agent to get rid of any trace Cu that might be adhering to the tank? You would want to do it while the tank is empty of anything living, as EDTA will also chelate Ca and Mg and other "good" metal ions, but the thing about EDTA is that once it has chelated to the metal ion, you can just wash the EDTA-Cu complex away. And since reefers usually add PLENTY of calcium to a tank, it wouldn't really matter if there was a little left over in the tank, it would disappear after a few water changes.

The EDTA might also "draw" the Cu out of the glass and silicone etc, as it would bind up free Cu and then the equilibrium would reestablish itself, releasing more Cu from the glass/silicone etc into the water. I could imagine soaking a tank in a solution of EDTA (for days, possible changing the EDTA solution a couple of times?) as a way to clean the tank before setting it up.

There are also other metal chelators out there, EDTA is just the most common. It is used for lead poisoning (you actually drink a solution of EDTA, and the EDTA-Pb complex is excreted).

Am I nuts?
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Get Jay to try it out.... ;)

Just have mike tell him to do it.... :funny:
How about a sledge hammer and $99 to buy a new 55 gallon.... :)

Nothing better than relieving stress and curing the problem of a Copper Riddled tank....
If it's leeching out by diffusion, one would only need so much as the equivelent of copper plauging the tank. As copper bonds with the EDTA, more would diffuse out to fill the void.

Quantifying the time requirements for treatment would be dependant upon the rate of difusion.

The troubling thing is, with difusion, are you ever going to be truly rid of the copper?

Before hypothesizing on a remedy, we need to define the process by which the copper is released into the water.
Understanding the enemy is the key to conquering him.... :)
Somewhere behind my street slang and crude sense of humor I hide my IQ.... ;)

You mean you forgot to empty the tank before ya poked a hole ni it??? :eek: :funny:
Back to what I was saying.... In what state does the copper exist within the environment?

If we define the state of coppers existance within the inorganic material environment, we can establish some criteria in which to determine the propper approach for it's removal....

By telling me that since I ate a penny and pissed in the lake that when the fish dies that swam though my pee, his decomposed body is going to leave behind the minute remnats of the penny and therefore inflict more harm upon the next inhabitants is moot.... We're talking about inorganics here... ;)
Any idea what the active ingredients are?
Cleaned out....

and thanks Jimmer...

I've been reading a couple of papers on using an organic extractant referred to as HR... Also was reading up a bit on lignin, but not of much value as of yet.
Hmmmmmm.... This is interesting... ;)

Blue or 'type-1' copper proteins are small proteins which bind a single copper atom and which are characterized by an intense electronic absorption band near 600 nm [MEDLINE:84135769], [MEDLINE:93164266]. The most well known members of this class of proteins are the plant chloroplastic plastocyanins, which exchange electrons with cytochrome c6, and the distantly related bacterial azurins, which exchange electrons with cytochrome c551. This family of proteins also includes amicyanin from bacteria such as Methylobacterium extorquens or Thiobacillus versutus that can grow on methylamine; auracyanins A and B from Chloroflexus aurantiacus [MEDLINE:92202194]; blue copper protein from Alcaligenes faecalis; cupredoxin (CPC) from cucumber peelings [MEDLINE:93106154]; cusacyanin (basic blue protein; plantacyanin, CBP) from cucumber; halocyanin from Natrobacterium pharaonis [MEDLINE:94253046], a membrane associated copper-binding protein; pseudoazurin from Pseudomonas; rusticyanin from Thiobacillus ferrooxidans [MEDLINE:91348256]; stellacyanin from the Japanese lacquer tree; umecyanin from horseradish roots; and allergen Ra3 from ragweed. This pollen protein is evolutionary related to the above proteins, but seems to have lost the ability to bind copper. Although there is an appreciable amount of divergence in the sequences of all these proteins, the copper ligand sites are conserved.
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I vote for Jay to try it.... cause I ain't gonna dose a tank with copper to try it out... ;)
Or you can try cucumber rinds... ;)

Read the info I posted...

but in a nutshell.....

Blue or 'type-1' copper proteins are small proteins which bind a single copper atom and which are characterized by an intense electronic absorption band near 600 nm. This family of proteins also includes cupredoxin (CPC) from cucumber peelings; cusacyanin (basic blue protein; plantacyanin, CBP) from cucumber;


It'd be worth chopping up a bunch of cucumber, putting it in a filter bag and soaking it with something......
plantacyanin also exists within spinach...

It didn't say if it was biological or not...
Crystal structure of plantacyanin, a basic blue cupredoxin from spinach
Oliver Einsle1, , Zara Mehrabian2, Robert Nalbandyan2 and Albrecht Messerschmidt1

(1) Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, 82152 Martinsried, Germany
(2) University of Maryland, School of Medicine, Anesthesiology Department, W. Baltimore St., Baltimore, MD 21201, USA

The crystal structure of the basic blue protein (plantacyanin) from spinach (SBP) has been solved to a resolution of 2.05 Å by molecular replacement using the homologous protein from cucumber (CBP) as a model. Although the sequence identity of 58% between both proteins is only moderate, the three-dimensional structures turned out to be highly similar and the buried residues, which form the hydrophobic core of the protein, are almost completely conserved. However, the redox potentials of both proteins differ by 40 mV, and a comparison of the two structures leads to a single lysine replacing a proline in the cucumber sequence, which causes a shift of the peptide chain and thus a subtle distortion of the copper ligand geometry in respect to CBP. The crystal contained three monomers of SBP in the asymmetric unit which show considerable variations in outer loop regions owing to crystal packing, but not in the regions presumed to be essential for redox partner recognition and redox potential fine tuning of the copper centers. Still, bond length variations at the copper site are at the same scale between the monomers of SBP as they are in respect to CBP, indicating that in the oxidized state the protein does not impose a high conformational strain on the copper.
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VII-D-1 Reduction and Oxidation Processes of Blue Copper Proteins, Azurin, Pseudoazurin, Umecyanin, Stellacyanin, Plantacyanin, And Plastocyanin Approached by Cyclic and Potential Step Voltammetries
Takeshi SAKURAI, Fumitaka NOSE, Takayuki FUJIKI and Schinnichiro SUZUKI (Osaka Univ.)

[Bull. Chem. Soc. Jpn. 69, 2855 (1996)]

Direct electrochemistry of a series of blue copper proteins: azurin, pseudoazurin, umecyanin, stellacyanin, plantacyanin, and plastocyanin has been performed at a gold electrode modified with di-4-pyridyl disulfide and/or at a bare glassy carbon electrode. Well-resolved cyclic voltammograms with peak separation, (DELTA)Ep = 55 - 100 mV were obtained. Protein molecules associate with the electrode surface through both electrostatic and hydrophobic interactions, of which the predominant one differs according to the combination of protein and electrode. Double-step voltammetry showed that redox processes of blue copper proteins depend profoundly on the translocation of the molecules (diffusion and/or change of orientation) at the electrode surface. The heterogeneous rate constants at pH 6.0 and 25 °C for both reduction and oxidation processes were independently determined to be the order of 10-3 to 10-4 cms-1 by single-step voltammetry and were compared with those determined by cyclic voltammetry. Further, activation parameters for redox processes of some blue copper proteins have been determined from temperature dependence studies. The reaction pathway of blue copper proteins was discussed.
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