Abstract
Protein reducing agents dithiothreitol (DTT) or tris(2-carboxyethyl)phosphine (TCEP) are crucial to disrupt disulfide bonds for qualitative and quantitative analysis in proteomics. Protein bond disruption is very important for analyzing proteins as single subunits. The electrochemical oxidation mechanism of DTT and TCEP was investigated using cyclic and differential pulse voltammetry over a wide pH range on a glassy carbon electrode. The oxidation mechanism of both compounds is irreversible, pH-dependent and proceeds in a single step. The anodic oxidation of DTT is associated with the oxidation of the sulfhydryl group with lowest pKa, while the anodic oxidation of TCEP is associated with the oxidation of the phosphine group in the molecule. The diffusion coefficients of DTT and TCEP were calculated, and the redox mechanisms are proposed.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
