Metal transportation
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We didn't want the metal ions to be uptaken by the cells since we want to transport specific metal ions (eg. radioactive ones) so we focused on putting metal-binding domains on the surface of the bacterial cells. This can be done by adding short metal-binding domains to bacterial constitutively expressed transmembrane proteins such as LamB or OmpC. | We didn't want the metal ions to be uptaken by the cells since we want to transport specific metal ions (eg. radioactive ones) so we focused on putting metal-binding domains on the surface of the bacterial cells. This can be done by adding short metal-binding domains to bacterial constitutively expressed transmembrane proteins such as LamB or OmpC. | ||
| - | '''Ref:'''Engineering the ''Escherichia coli'' outer membrane protein OmpC for metal bioadsorption, Norberto Cruz, Sylvie Le Borgne, Georgina Hern´andez-Ch´avez, Guillermo Gosset, Fernando Valle & Francisco Bolivar, 2000, Biotechnology Letters, 22 | + | '''Ref:''' Engineering the ''Escherichia coli'' outer membrane protein OmpC for metal bioadsorption, Norberto Cruz, Sylvie Le Borgne, Georgina Hern´andez-Ch´avez, Guillermo Gosset, Fernando Valle & Francisco Bolivar, 2000, Biotechnology Letters, 22 |
For the metal transportation to occur the cells should adsorp metal ions at a specific location and release them at another specific loaction. In order to achieve this we planned to use the pH dependence of the metal-binding domains for their affinity for metals. | For the metal transportation to occur the cells should adsorp metal ions at a specific location and release them at another specific loaction. In order to achieve this we planned to use the pH dependence of the metal-binding domains for their affinity for metals. | ||
| - | + | We need at least a semi-solid media for bacterial cell movement. Thus, we cannot use a constant pH gradient in the medium due to diffusion. | |
| + | |||
| + | We decided to use the bacteriorhodopsin molecule, which, we think, will create a pH decrease at the surface of the cells if the cells are illuminated with a specific wavelength of light. This sudden pH decrease will cause the metal-binding domains to release the metals that they have previously bound. So the loaction that we want the cells to release the metals should be specifically illuminated with a specific wavelength. | ||
Revision as of 21:00, 15 October 2007
- In this project our aim is to transport specific metal ions from a specific location to another on the surface of engineered bacterial cells. In other words, to use cells as metal carriers.
We didn't want the metal ions to be uptaken by the cells since we want to transport specific metal ions (eg. radioactive ones) so we focused on putting metal-binding domains on the surface of the bacterial cells. This can be done by adding short metal-binding domains to bacterial constitutively expressed transmembrane proteins such as LamB or OmpC.
Ref: Engineering the Escherichia coli outer membrane protein OmpC for metal bioadsorption, Norberto Cruz, Sylvie Le Borgne, Georgina Hern´andez-Ch´avez, Guillermo Gosset, Fernando Valle & Francisco Bolivar, 2000, Biotechnology Letters, 22
For the metal transportation to occur the cells should adsorp metal ions at a specific location and release them at another specific loaction. In order to achieve this we planned to use the pH dependence of the metal-binding domains for their affinity for metals.
We need at least a semi-solid media for bacterial cell movement. Thus, we cannot use a constant pH gradient in the medium due to diffusion.
We decided to use the bacteriorhodopsin molecule, which, we think, will create a pH decrease at the surface of the cells if the cells are illuminated with a specific wavelength of light. This sudden pH decrease will cause the metal-binding domains to release the metals that they have previously bound. So the loaction that we want the cells to release the metals should be specifically illuminated with a specific wavelength.
