Reaction of Adsorbed RNAse on a Mercury Electrode

Pavlović, O.; Miller, I.R.

doi:10.1007/978-3-0348-5848-9_49

Cited by 21 publications

(5 citation statements)

References 8 publications

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“…The decrease in Q for the oxidative CCCP measurements relative to the PSA measurements are consistent with an alteration of the conformation of sulfhydryl groups formed from the reduction of the disulfide bonds which occurs in the absence of oxygen that has been reported by other workers [30,311. These results may indicate that extended periods at the electrolysis potential leads to a reorientation of the sulfhydryl groups to a conformation that geometrically prohibits their oxidation to a disulfide bond.…”

Section: Resultssupporting

confidence: 78%

The potentiometric stripping analysis of proteins

Honeychurch

Ridd

1996

Electroanalysis

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Ten proteins were analyzed by potentiometric stripping analysis (PSA) following reductive accumulation on a HMDE and oxidation with dissolved oxygen. During the reductive accumulation period the surface disulfide bonds are reduced to sulfhydryl pairs. The rate of oxidation of the sulfhydryl pairs is determined by the transport of dissolved oxygen to the electrode surface. Comparison of the PSA response to that obtained by constant (current chronopotentiometry (CCCP) of the reduced protein in a deoxygenated solution showed that the prescnce of dissolved oxygen, in the PSA experiments stabilized the proteins from further conformational changes following the reduction of the surface disulfide bonds.

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Section: Resultssupporting

confidence: 78%

The potentiometric stripping analysis of proteins

Honeychurch

Ridd

1996

Electroanalysis

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“…1, curves 1-10) at Ϫ0.85 V. The increase in capacitance at this potential with increasing c p indicates that reduced forms of RNase A are less strongly adsorbed than disulfidic ones. This observation agrees with an earlier one (13,14) in which the pseudocapacitance peak of RNase A at pH 1.0 was linked to the reduction of two -S-Sbonds. At pH 8.8 used in this study the faradaic peak at Ϫ0.85 V (Fig.…”

Section: Resultssupporting

confidence: 92%

“…The molecule is very stable in solution, with a Gibbs energy of denaturation of about 61 Ϯ 8 kJ/mol (12). The ac polarographic investigation of lysozyme interaction with DME shows, in addition to a desorption peak, a second peak at about Ϫ0.80 V, ascribed to rearrangement of the adsorbed molecules or to reversible reduction of disulfide groups (13).…”

mentioning

confidence: 98%

Adsorption of Ribonuclease A and Lysozyme at the Mercury/Solution Interface

Vidić

Sužnjević

Erceg

et al. 1999

Microchemical Journal

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“…Pavlovic and Miller [52] studied native and denatured ribonuclease by AC polarography. They suggested the following mechanism for their results involving À S À S À groups:…”

Section: Peak Smentioning

confidence: 99%

Electroactivity of Avidin and Streptavidin. Avidin Signals at Mercury and Carbon Electrodes Respond to Biotin Binding

2004

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Avidin and streptavidin were studied by phase-sensitive AC and cyclic voltammetry as well as by constant current chronopotentiometry at mercury (in alkaline media) and carbon electrodes (in acid medium). In contrast to the generally accepted belief that these proteins are electroinactive, we observed various electrochemical responses at these electrodes. Both proteins produced peaks due to oxidation of tyrosine and tryptophan residues at carbon electrodes and a catalytic peak H at a hanging mercury drop electrode. At the latter electrode avidin produced phasein AC voltammetric and cyclic voltammetric peaks close to À 0.6 V (peak S) which were assigned to Hg-S interactions, involving cystine/cysteine residues. In cobalt containing solution avidin produced a characteristic catalytic double wave requiring presence of cystine/cysteine residues in the protein molecule. Streptavidin, which does not contain these residues, yielded neither the catalytic double wave nor peak S. All the above avidin signals responded to biotin binding; peak S increased (up to 4 biotin molecules bound) while other avidin signals decreased as a result of biotin binding. A tentative scheme of interfacial behavior of avidin and avidin-biotin complex, depending on the electrode charge, was suggested.

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Reaction of Adsorbed RNAse on a Mercury Electrode

Cited by 21 publications

References 8 publications

The potentiometric stripping analysis of proteins

The potentiometric stripping analysis of proteins

Adsorption of Ribonuclease A and Lysozyme at the Mercury/Solution Interface

Electroactivity of Avidin and Streptavidin. Avidin Signals at Mercury and Carbon Electrodes Respond to Biotin Binding

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