Enzymatic activity and catalytic hydrogen evolution in reduced and oxidized urease at mercury surfaces

Protein structural transition at negatively charged electrode surfaces. Effects of temperature and current density

“…Considering our previous results [7,16] we have to take in account also other conditions, not only the ionic strength, influencing the depth of the outer double layer and modifying the electric field effects on the given surface-attached protein.…”

“…Moreover it can be expected that temperature, which influences the stability and dynamics of the surface-attached protein [16], can affect the outcome of the electric field action on the surfaceattached protein. Thus the protein structural transition at the electrode surface should depend not only on the ionic strength but also on temperature and current density.…”

Electrochemistry of Nonconjugated Proteins and Glycoproteins. Toward Sensors for Biomedicine and Glycomics

“…An atomically smooth surface of liquid mercury makes it possible to prepare pinhole-free monolayers of thiolated DNAs 237 and of other thiols 161 to obtain chemically modified electrodes for protein analysis. 105 , 228 , 238 − 240 Smooth surfaces can be prepared also by forming a miniature liquid Hg meniscus at SAE. Moreover, strong hydrophobicity and other properties of Hg electrodes differ from most of the solid electrodes predominantly used in EC analyses.…”

“…CPS peak H of proteins appears at highly negative potentials, such as −1.8 V (against Ag/AgCl electrode). To reach this potential, the surface-attached protein is exposed to the electric field effects at negative potentials causing unfolding/denaturation of the native protein 238 or dissociation/disintegration of the DNA–protein complex. 240 It has been shown that such damage to the surface-attached biomacromolecules depends strongly on the time of their exposure to negative potentials and can be avoided at highly negative I s tr intensities (sections 5.3 and 7.5 ), inducing very high rates of potential changes and thus very short exposure times.…”

“…Moreover, CPS analysis of proteins can mostly be performed under air. 155 , 230 , 231 , 238 , 239 , 254 …”