Effect of Surfactants on the polarographic Brdicka activity of cysteine

doi:10.1016/0302-4598(77)80042-1

Bioelectrochemistry and Bioenergetics

Volume 4, Issue 4, 1977, Pages 413-424

Bioelectrochemistry ...

https://doi.org/10.1016/0302-4598(77)80042-1 Get rights and content

Abstract

The catalytic brdička activity of cysteine is greatly modified by a number of electrochemically inactive surfactants. Regardless of their chemical nature and electrical charge, all surfactants which are adsorbed at the electrode surface also at potentials of the brdička catalytic hydrogen wave bring about a gradual increase in the height of the brdička currents at low degree of coverage of the electrode surface by the adsorbed surfactant. When the degree of this coverage exceeds a certain value, the stimulating effect gradually diminishes with further increasing surfactant concentration. Finally, when the electrode becomes fully covered, the brdička currents become suppressed compared to their magnitude in the complete absence of the surfactant. The possibility of the self—modifying effect of the proteinic catalysts on their brdička catalytic activity is discussed.

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Cited by (7)

Development and evaluation of a glassy carbon electrode modified with silver and mercury nanoparticles for quantification of cysteine rich peptides
2017, Sensors and Actuators, B: Chemical
Citation Excerpt :
The interest in these peptides lies in the following general facts: they have been shown to be part of a defense mechanism by plants and animals in response to exposure to high levels of essential and non-essential metals (Pb as an example); the presence of these peptides in concentrations above certain limits in living organisms could be associated to resistance of such organisms to certain therapies against cancer [12,17–24]. Most studies reported involving Brdičkás reaction have been performed using a dropping mercury electrode (DME), a static mercury drop electrode, (SMDE) [24–26] or a hanging drop mercury electrode (HDME) [19]. However, these electrodes are not at all convenient when the determinations have to be carried out directly in the field because they are not amenable to miniaturization, do not provide results in real time and because their use brings about the possibility of ambient contamination with relatively high amounts of mercury either in liquid or gaseous form.
A glassy carbon electrode,covered with a Nafion film, on which nano-structured bimetallic particles of Ag-Hg were deposited; from now on “the AgHgNpNf/GC electrode”, was used for the indirect determination of cysteine, glutathione and metallothioneins by measuring the catalytic hydrogen evolution signal according to the Brdička reaction using cobalt as a catalyst. Upon successful formation and deposition of the Ag-Hg bimetallic nanoparticles cyclic voltammetry (CV), scanning electron microscopy (SEM) and atomic force microscopy (AFM) were used to characterize the electrode for that specific task. The results showed the electrode to be mechanically resistant even under sonication, stable in its performance, porous, sensitive in its response and of low cost to be built. Differential pulse voltammetry signals for cysteine and glutathione obtained using the AgHgNpNf/GC electrode were qualitatively similar to those reported using a hanging mercury drop electrode, (HMDE), dropping mercury electrode (DME) and static mercury drop electrode (SMDE). Detection limits based on the variability of a blank solution, (3 s criterion) calculated for those tests were 0.463 μg L⁻¹ and 0.064 μg L⁻¹, for cysteine and glutathione, respectively. Based on the Brdička procedure and considering the particular characteristics of the new electrode, some analytical tests were carried out for the indirect determination of the metallothioneins content of samples of blood serum of rats exposed to lead by measuring the evolution of the catalytic hydrogen signal. An average accuracy value around 102%, n = 6, and a precision of 0.87% ± 0.09 were obtained for these tests.
Electrochemical behavior of phytochelatins and related peptides at the hanging mercury drop electrode in the presence of cobalt(II) ions
2006, Bioelectrochemistry
Direct current voltammetry and differential pulse voltammetry have been used to investigate the electrochemical behaviour of two phytochelatins: heptapeptide (γ-Glu–Cys)₃–Gly and pentapeptide (γ-Glu–Cys)₂–Gly, tripeptide glutathione γ-Glu–Cys–Gly and its fragments: dipeptides Cys–Gly and γ-Glu–Cys at the hanging mercury drop electrode in the presence of cobalt(II) ions. Most interesting results were obtained with direct current voltammetry in the potential region of − 0.80 V up to − 1.80 V. Differential pulse voltammetry of the same solutions of Co(II) with peptides gives more complicated voltammograms with overlapping peaks, probably in connection with the influence of adsorption at slow scan rates necessarily used in this method. However, in using Brdička catalytic currents for analytical purposes, differential pulse voltammograms seem to be more helpful. Presented investigations have shown that particularly the prewave of cobalt(II) allows distinguishing among phytochelatins, glutathione, and its fragments.
Catalytic Hydrogen Evolution at Mercury Electrodes from Solutions of Peptides and Proteins
2005, Perspectives in Bioanalysis
Citation Excerpt :
By decrease of temperature, by addition of surfactants or by increase of ammonia concentration, the double wave changes into a single maximum (Figure 13) (Marha, 1957; Lamprecht and Katzlmeier, 1961; Alexandrov et al., 1963). The occurrence of the two maxima in the double wave has been tentatively explained either (a) by catalytic action of different amino acids in the protein molecule (Müller, 1955), (b) by different tertiary structure of proteins (Iwanow, 1961), (c) by two different cobalt complexes of the protein (Mairanovskii and Mairanovskaia, 1961) or (d) by the protein catalyst acting first in adsorbed and then in desorbed state (Berg, 1964, 1966; cf. Mader and Veselá, 1977). In general, adsorption of the protein at the electrode plays an important role in the mechanism of Brdička catalytic reaction (Senda et al., 1976; Kolthoff et al., 1978).
The catalytic evolution of hydrogen at electrodes is catalyzed by a great variety of species, among others, by peptides and proteins; when carried out on small laboratory scale, it can become a useful way for studying physio-chemical properties of the catalysts, as well as for their sensitive quantitative determination. This chapter discusses the aspect of the general electrochemical reaction of peptides and proteins. Peptides and proteins can cause the catalytic evolution of hydrogen on mercury electrodes as catalysts of both categories ((1) organic molecules or ions containing nitrogen atom with a free electron pair, alone or together with thiolic sulfur; and (2) reduced forms of various transition metal complexes with particular ligands), provided they contain catalytically active groups or form catalytically active complexes with appropriate cations. Although the first experience with catalytic evolution of hydrogen on mercury electrodes was gained with the “presodium” current, the great majority of results in research and in practical applications of electrochemical activity of peptides and proteins have been based on hydrogen evolution catalyzed by their complexes with cobalt ions. Only the renewed, successful attempts to catalyze hydrogen evolution by complexes of metals other than cobalt and the recent discoveries based on catalytic hydrogen evolution in absence of cobalt have spurred new development of the specific field of peptide and protein electrochemistry. The inexpensive electrochemical apparatus offers very sensitive methods for the study and analysis of peptides and proteins.
Catalytic hydrogen activity of the low-molecular weight thiols: kinetic control of the brdička catalytic current
1982, Electrochimica Acta
At sufficient excess of cobalt, the Brdička polarographic catalytic hydrogen currents of low molecular weight thiols frequently exhibit typical kinetic characteristics. A detailed investigation of these currents has revealed also a marked adsorption component. A mechanism which leads to the formation of the Brdička currents was suggested on the basis of the changes of these currents with a number of factors. Under the speicified conditons the Brdička catalytic wave may be distorted; the observed deformations are either due to the modification of the proper Brdička current, or they are a consequence of the simultaneous appearance of another type of the catalytic hydrogen current, which can also exist in the transition metal/ligand systems.
403 - Polarographic studies on proteins
1981, Bioelectrochemistry and Bioenergetics
Basic information concerning the behavior, on electrochemical reduction and oxidation, of proteins and enzymes at a mercury electrode and other electrodes is summarized. The electrochemical behavior of ferredoxin at a mercury electrode is interpreted on the basis of the theory of surface redox reaction.
Equations of Brdička current at a d.m.e. and a h.m.d.e. of SS/SH-containing proteins are presented in which the Brdička current activity of protein is represented by a constant k_B-Values of k_B of various proteins are given. Cytochrome c and myoglobin contain neither the SS nor the SH group, but give a Brdička current which is attributable to the heme moiety in the molecules. The Brdička current can be utilized for the study of protein-protein interaction, as well as for trace analysis of proteins. Other polarographic methods of trace analysis of proteins are summarized.
Polarographic studies on proteins
1981, Journal of Electroanalytical Chemistry
Basic information concerning the behavior, on electrochemical reduction and oxidation, of proteins and enzymes at a mercury electrode and other electrodes is summarized. The electrochemical behavior of ferredoxin at a mercury electrode is interpreted on the basis of the theory of surface redox reaction.
Equations of Brdička current at a d.m.e. and a h.m.d.e. of SS/SH-containing proteins are presented, in which the Brdička current activity of protein is represented by a constant k_B. Values of k_B of various proteins are given. Cytochrome c and myoglobin contain neither the SS nor the SH group, but give a Brdička current which is attributable to the heme moiety in the molecules. The Brdička current can be utilized for the study of protein-protein interaction, as well as for trace analysis of proteins. Other polarographic methods of trace analysis of proteins are summarized.

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^☆: Discussed at the Symposium on “Biopolymers in Adsorbed State” held at Weimer (D.D.R.), 26–28 April 1977.

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Effect of Surfactants on the polarographic Brdicka activity of cysteine☆

Abstract

Abh. Dtsch. Akad. Wiss. Berlin, Elektrochem. Meth. Prinz. Molekular—Biologie

Bioelectrochem. Bioenerg.

Ann. Biol. Clin. (Paris)

Bull. Chem. Soc. Japan

Bull. Chem. Soc. Japan

Anal. Chem.