I work with metalloenzymes with reasonable reduction potentials, between -0.1 and +0.4 V vs. NHE, that I constantly run on native PAGE gels. I've noticed they don't change color during electrophoresis (~200 V applied), indicating the oxidation state of the metal is preserved. I understand this is not the same as doing electrochemistry using a working electrode, etc, but I don't understand fundamentally why the metals don't become oxidized/reduced when there is an applied potential and current flowing across the gel which they inhabit.
Any thought's on this would be very much appreciated by a curious grad student.
In the gel, you have a flow of ions, not free electrons. In addition, your sample is fully reduced by DTT or ßME. Proteins could be oxidised by air oxygen (slow diffusion through the gel) or by rests of the APS from the polymerisation chemistry (which is why gels after polymerisation should be stored for 24 h in the fridge before use).
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