Analysis of HypD disulfide redox chemistry via optimization of fourier transformed ac voltammetric data
Rapid disulfide bond formation and cleavage is an essential mechanism of life. Using large amplitude Fourier transformed alternating current voltammetry (FTacV) we have measured previously uncharacterized disulfide bond redox chemistry in Escherichia coli HypD. This protein is representative of a cl...
| Main Authors: | , , , , , , , , , , |
|---|---|
| Format: | Journal article |
| Published: |
American Chemical Society
2016
|