Team:Chiba/Project/oxidation
From 2013.igem.org
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<h2 id="oxidation" style="background-color:#ff9933"><center>oxidation</center></h2> | <h2 id="oxidation" style="background-color:#ff9933"><center>oxidation</center></h2> | ||
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So, we thought changing the E.coli cytosol to oxidative state like yeast leads to be attracted by magnets.<br> | So, we thought changing the E.coli cytosol to oxidative state like yeast leads to be attracted by magnets.<br> | ||
That's why knocking out trxB and gor is neccesary to acchive magnetism. | That's why knocking out trxB and gor is neccesary to acchive magnetism. | ||
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</p> | </p> | ||
- | + | <h3>2. | |
Revision as of 10:03, 26 September 2013
oxidation
1.Introduction
Two proteins called glutathione and thioredoxin which have disulfide bond (-s-s-) in oxidized states exist in E.coli(WT). They play a role of redox control in E.coli.
Oxidative stress avtivates glutathione reductase (gor) and thioredoxin reductase (trxB). Therefore, E.coli is constantly reductive.
On the other hand, cytosol of yeast is oxidative originally and they can have magnetism, and be attracted by magnets.
So, we thought changing the E.coli cytosol to oxidative state like yeast leads to be attracted by magnets.
That's why knocking out trxB and gor is neccesary to acchive magnetism.