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Team:Chiba/oxydation/redox homeostasis
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It is known that Oxidative stress (ex. from ultra violet or oxidant) activates glutathione and thioredoxin. | It is known that Oxidative stress (ex. from ultra violet or oxidant) activates glutathione and thioredoxin. | ||
(Ref. Nakamura H, Nakamura K, Yodoi J: Redox regulation of cellular activation. Ann. Rev. Immuol., 15: 351-369, 1997)<br> | (Ref. Nakamura H, Nakamura K, Yodoi J: Redox regulation of cellular activation. Ann. Rev. Immuol., 15: 351-369, 1997)<br> | ||
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Based on these factors, we expected that if we knock down gor and trxB, disulfide bond in matrix protein would be remained and inside E. coli would be oxidant. That means iron can be in form of Fe<sub>3</sub>O<sub>4</sub>, and have magnetism.<br> | Based on these factors, we expected that if we knock down gor and trxB, disulfide bond in matrix protein would be remained and inside E. coli would be oxidant. That means iron can be in form of Fe<sub>3</sub>O<sub>4</sub>, and have magnetism.<br> | ||
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Latest revision as of 01:21, 28 September 2013
E. coli Redox Homeostasis
It is known that Oxidative stress (ex. from ultra violet or oxidant) activates glutathione and thioredoxin.
(Ref. Nakamura H, Nakamura K, Yodoi J: Redox regulation of cellular activation. Ann. Rev. Immuol., 15: 351-369, 1997)
Glutathione and thioredoxin acts as an electron donor, and does reduction of all disulfide bond (formed in cellular protein) into cysteine.
Besides, NADPH and the two reductase, glutathione reductase (gor) and thioredoxin-disulfide reductase (trxB) reduces glutathione and thioredoxin. From this, disulfide bond in matrix protein would be reduced into -SH HS and the redox state inside the cell would be reductive.
Based on these factors, we expected that if we knock down gor and trxB, disulfide bond in matrix protein would be remained and inside E. coli would be oxidant. That means iron can be in form of Fe3O4, and have magnetism.
