Direct electron transfer between copper-containing proteins and electrodes (original) (raw)
Gold-Decorated Carbon Composite Electrodes for Enzymatic Oxygen Reduction
Electroanalysis, 2012
Functional composites of carbon and gold nanoparticles create a hierarchical architecture that facilitates high enzyme loading. Subsequent immobilization of the multicopper oxidase, Trametes versciolor laccase, was optimal with dithiobis-(succinimidyl propionate), due to the formation of thiol bonds between the protein molecules and gold. The immobilized laccase catalyzed oxygen reduction, with an onset potential of~0.6 V (vs. Ag/AgCl), indicated effective orientation of the enzyme redox center to enable direct electron transport between enzyme and the composite electrode. Current densities in half-cell configurations provide scalable outputs of 50-80 mA/cm 2 with the optimized electrode design. The methodology herein describes a rapid, facile preparation of gold-decorated carbon composite materials for use as electrode scaffolds that can be integrated into a range of bioelectronic devices.
Self-powered wireless carbohydrate/oxygen sensitive biodevice based on radio signal transmission
PloS one, 2014
Here for the first time, we detail self-contained (wireless and self-powered) biodevices with wireless signal transmission. Specifically, we demonstrate the operation of self-sustained carbohydrate and oxygen sensitive biodevices, consisting of a wireless electronic unit, radio transmitter and separate sensing bioelectrodes, supplied with electrical energy from a combined multi-enzyme fuel cell generating sufficient current at required voltage to power the electronics. A carbohydrate/oxygen enzymatic fuel cell was assembled by comparing the performance of a range of different bioelectrodes followed by selection of the most suitable, stable combination. Carbohydrates (viz. lactose for the demonstration) and oxygen were also chosen as bioanalytes, being important biomarkers, to demonstrate the operation of the self-contained biosensing device, employing enzyme-modified bioelectrodes to enable the actual sensing. A wireless electronic unit, consisting of a micropotentiostat, an energy ...
Journal of Materials Chemistry, 2012
An electrochemically functionalized surface of p-type silicon was used as a nanostructured material for immobilization and activation of a redox metalloprotein. A protocol resulting in the stable enzyme adsorption and utilization was applied to Trametes versicolor laccase (TvL), the ''blue'' coppercontaining oxidase enzyme, a model bio-electrocatalyst for oxygen reduction. The obtained system was tested as a photocatalytic electrode for oxygen sensing through its electroreduction at copper ionic active sites following illumination with visible light. Processes related to the photoexcitation and charge separation occur within the semiconductor (SC) material. Direct, rather than mediated by 2,2 0azinobis(3-ethylbenzothiazoline-6-sulfonate) (ABTS), electron transfers from the semiconductor to the enzyme were observed. The topography of the p-Si substrate was assessed by transmission electron microscopy (TEM) and tapping mode atomic force microscopy (TM AFM) methods. The electronic properties of the systems were tested using synchrotron radiation photoelectron spectroscopy (SRPES). The nature of the biomolecule immobilization was studied by TM AFM.
Electroanalysis, 2011
... Thomas Beneyton 1, ,; Yvonne Beyl 2,3, ,; Dmitrii A. Guschin 2,3 ,; Andrew D. Griffiths 1 ,; Valerie Taly 1 ,; Wolfgang Schuhmann 2,3,*. Article first published online: 21 JUN 2011. DOI: 10.1002/elan.201100054. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim ...
Systems and synthetic biology, 2011
The de novo engineering of new proteins will allow the design of complex systems in synthetic biology. But the design of large proteins is very challenging due to the large combinatorial sequence space to be explored and the lack of a suitable selection system to guide the evolution and optimization. One way to approach this challenge is to use computational design methods based on the current crystallographic data and on molecular mechanics. We have used a laccase protein fold as a scaffold to design a new protein sequence that would adopt a 3D conformation in solution similar to a wild-type protein, the Trametes versicolor (TvL) fungal laccase. Laccases are multi-copper oxidases that find utility in a variety of industrial applications. The laccases with highest activity and redox potential are generally secreted fungal glycoproteins. Prokaryotic laccases have been identified with some desirable features, but they often exhibit low redox potentials. The designed sequence (DLac) shares a 50% sequence identity to the original TvL protein. The new DLac gene was overexpressed in E. coli and the majority of the protein was found in inclusion bodies. Both soluble protein and refolded insoluble protein were purified, and their identity was verified by mass spectrometry. Neither protein exhibited the characteristic T1 copper absorbance, neither bound copper by atomic absorption, and neither was active using a variety of laccase substrates over a range of pH values. Circular dichroism spectroscopy studies suggest that the DLac protein adopts a molten globule structure that is similar to the denatured and refolded native fungal TvL protein, which is significantly different from the natively secreted fungal protein. Taken together, these results indicate that the computationally designed DLac expressed in E. coli is unable to utilize the same folding pathway that is used in the expression of the parent TvL protein or the prokaryotic laccases. This sequence can be used going forward to help elucidate the sequence requirements needed for prokaryotic multi-copper oxidase expression. The online version of this article (doi:10.1007/s11693-011-9080-9) contains supplementary material, which is available to authorized users.
Electroanalysis, 2013
14 Single-and multi-walled carbon nanotubes from different sources were characterized in detail, and the characteristics obtained were carefully analyzed. The carbon material with the highest capacitance, and also other superior properties ("Taunit-M" from "NanoTechCenter", Russia), was chosen for further modification and fabrication of buckypaper based electrodes. These electrodes were biomodified with plant and fungal laccases, as well as fungal bilirubin oxidase. The designed biocathodes were investigated in simple buffers and also in a complex physiological fluid (human serum). Biocathodes based on immobilized fungal laccase were bioelectrocatalytically inactive in chloride containing media at neutral pH. In spite of the quite high current densities realized using biodevices based on plant laccase and fungal bilirubin oxidase, the limited thermal stability of the enzymes renders the biocathodes inadequate for practical applications in implanted situations.
Comparative analysis of spatial organization of laccases from Cerrena maxima and Coriolus zonatus
Crystallography Reports, 2007
Laccase (oxygen oxidoreductase, EC 1.10.3.2) belongs to the multicopper oxidase family. The main function of this enzyme is to perform electron transfer from the oxidized substrate through the mononuclear copper-containing site T 1 to the oxygen molecule bound to the site T 3 in the trinuclear T 2/ T 3 cluster. The structures of two new fungal laccases from C. maxima and C. zonatus were solved on the basis of synchrotron X-ray diffraction data. Both laccases show high structural homology with laccases from other sources. The role of the carbohydrate component of laccases in structure stabilization and formation of ordered protein crystals was demonstrated. In the structures of C. maxima and C. zonatus laccases, two water channels of functional importance were found and characterized. The structural results reported in the present study characterize one of the functional states of the enzyme fixed in the crystal structure.
Immobilization of galactose oxidase on self-assembled monolayers of thiols on Au and Ag surfaces
Journal of Raman Spectroscopy, 2012
Galactose oxidase (GalOD) was immobilized on self-assembled monolayers of thiols on silver and gold surfaces using trans-stilbene (4,4′-diisothiocyanate)-2,2′disulphonic acid (DIDS) as the bridging compound. DIDS is the symmetrical bifunctional reagent that reacted with the amine moiety of the thiol and with primary amino groups of enzyme. The Raman measurement revealed that onto cysteamine-modified silver and gold electrodes, bands corresponding to the galactose oxidase (about 694, 1076, 1274 cm-1 on Au and 762, 1058, 1274 cm-1 on Ag) appeared and clearly demonstrated its immobilization onto Au and Ag surfaces. Simultaneously, we have also observed changes in the ratio of trans-gauche conformers of adsorbed cysteamine molecules. Layers revealing high content of trans conformer are transformed into layers composed mainly of cysteamine molecule in gauche conformation after galactose oxidase adsorption. These observations deliver a strong support for enzyme immobilization on cysteamine-modified gold and silver surfaces. The surface plasmon resonance experiment gave a surface coverage of~8.4 Â 10 7 g/cm 2 for gold electrode modified cysteamine using DIDS chemistry and 1.1 Â 10 7 g/cm 2 for the cysteamine only modified gold substrate and demonstrated that galactose oxidase layers immobilized with DIDS coupling reagent are quite stable and cannot be easily removed from the surface by treatment with a buffer solution. The surface plasmon resonance results indicated that in this method, a multilayer of galactose oxidase have been immobilized. Our new method of covalent attachment of enzymes seems to be quite promising as a new way of manufacturing biosensors.
Fundamentals, Applications, and Future Directions of Bioelectrocatalysis
Chemical Reviews
Bioelectrocatalysis is an interdisciplinary research field combining biocatalysis and electrocatalysis via the utilization of materials derived from biological systems as catalysts to catalyze the redox reactions occurring at an electrode. Bioelectrocatalysis synergistically couples the merits of both biocatalysis and electrocatalysis. The advantages of biocatalysis include high activity, high selectivity, wide substrate scope, and mild reaction conditions. The advantages of electrocatalysis include the possible utilization of renewable electricity as an electron source and high energy conversion efficiency. These properties are integrated to achieve selective biosensing, efficient energy conversion, and the production of diverse products. This review seeks to systematically and comprehensively detail the fundamentals, analyze the existing problems, summarize the development status and applications, and look toward the future development directions of bioelectrocatalysis. First, the structure, function, and modification of bioelectrocatalysts are discussed. Second, the essentials of bioelectrocatalytic systems, including electron transfer mechanisms, electrode materials, and reaction medium, are described. Third, the application of bioelectrocatalysis in the fields of biosensors, fuel cells, solar cells, catalytic mechanism studies, and bioelectrosyntheses of high-value chemicals are systematically summarized. Finally, future developments and a perspective on bioelectrocatalysis are suggested.
Scientific reports, 2018
Bipolar electrochemistry (BPE) has been lately explored as a simple, reliable and novel electrochemical technique for the adjustment of various conductive substrates. Herein, BPE is performed to derive both of cathode and anode electrodes for the development of mediatorless/membraneless biofuel cell (BFC). On one hand, a preferable substrate for immobilization of bilirubin oxidase enzyme is prepared based on the electropolymerization of thiophene-3-carboxcylic acid (TCA) on an Au microfilm as a bipolar electrode. The resulted biocathode as novel bioelectrocatalyst offers a high electrocatalytic activity toward direct oxygen reduction reaction (ORR) with onset potential and current density of 0.55 V (vs. Ag/AgCl) and 867 μA cm, respectively. On the other hand, another analogous Au bipolar electrode is electroplated through BPE to derive Au nanostructures (AuNSs). This modified Au electrode is utilized as an anodic platform for immobilization of flavin adenine dinucleotide-dependent g...
PLoS ONE, 2014
Typical multicopper oxidases (MCOs) have ten conserved histidines and one conserved cysteine that coordinate four copper atoms. These copper ions are required for oxidase activity. During our studies of insect MCOs, we discovered a gene that we named multicopper oxidase-related protein (MCORP). MCORPs share sequence similarity with MCOs, but lack many of the copper-coordinating residues. We identified MCORP orthologs in many insect species, but not in other invertebrates or vertebrates. We predicted that MCORPs would lack oxidase activity due to the absence of copper-coordinating residues. To test this prediction, we purified recombinant Tribolium castaneum (red flour beetle) MCORP and analyzed its enzymatic activity using a variety of substrates. As expected, no oxidase activity was detected. To study MCORP function in vivo, we analyzed expression profiles of TcMCORP and Anopheles gambiae (African malaria mosquito) MCORP, and assessed RNAimediated knockdown phenotypes. We found that both MCORPs are constitutively expressed at a low level in all of the tissues we analyzed. Injection of TcMCORP dsRNA into larvae resulted in 100% mortality prior to adult eclosion, with death occurring mainly during the pharate pupal stage or late pharate adult stage. Injection of TcMCORP dsRNA into pharate pupae resulted in the death of approximately 20% of the treated insects during the pupal to adult transition and a greatly shortened life span for the remaining insects. In addition, knockdown of TcMCORP in females prevented oocyte maturation and, thus, greatly decreased the number of eggs laid. These results indicate that TcMCORP is an essential gene and that its function is required for reproduction. An understanding of the role MCORP plays in insect physiology may help to develop new strategies for controlling insect pests.
New Class of Antimicrobial Agents: SBA-15 Silica Containing Anchored Copper Ions
Journal of Nanomaterials, 2017
The paper is about a new class of antimicrobial functional nanomaterials. Proposed compounds are based on SBA-15 porous silica matrices and contain anchored copper ions. Thanks to the immobilization of functional groups the compounds are safer for environment than commonly used disinfectant agents. We prepared and examined silica based materials containing two concentrations of copper-containing groups: 10 and 5%. For the reference we prepared samples containing free-standing CuO molecules in the structure and checked their antimicrobial properties. Antibacterial effect of considered SBA-15-Cu material was tested on Escherichia coli bacteria. Antimicrobial tests were applied for the pure form of the material and as modifying agents for plastics. The obtained results showed that the sample with lower concentration of active copper-containing groups has stronger antimicrobial properties than the one with higher concentration of copper. Interestingly, silica containing free-standing Cu...
Recent Developments of Nanostructured Electrodes for Bioelectrocatalysis of Dioxygen Reduction
Advances in Physical Chemistry, 2011
The recent development of nanostructured electrodes for bioelectrocatalytic dioxygen reduction catalysed by two copper oxidoreductases, laccase and bilirubin oxidase, is reviewed. Carbon-based nanomaterials as carbon nanotubes or carbon nanoparticles are frequently used for electrode modification, whereas there are only few examples of biocathodes modified with metal or metal oxide nanoparticles. These nanomaterials are adsorbed on the electrode surface or embedded in multicomponent film. The nano-objects deposited act as electron shuttles between the enzyme and the electrode substrate providing favourable conditions for mediatorless bioelectrocatalysis.
Fungal-mediated electrochemical system: Prospects, applications and challenges
Current Research in Microbial Sciences, 2021
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Frontiers in Chemistry, 2018
In recent years, enzymatic fuel cells have experienced a great development promoted by the availability of novel biological techniques that allow the access to a large number of enzymatic catalysts. One of the most important aspects in this area is the development of biocatalysts for the oxygen reduction reaction (ORR). Laccases from the group of enzymes called blue multi-cooper oxidases have received considerable attention because of their ability to catalyze the electrochemical oxygen reduction reaction to water when immobilized on metallic or carbonaceous electrode materials. In this paper we report a comprehensive study of the electrocatalytic activity of the enzyme Copper efflux oxidase (CueO) from Escherichia coli immobilized on different electrode materials. The influence of the electrode substrate employed for protein immobilization was evaluated using glassy carbon, gold or platinum electrodes. Gold and platinum electrodes were modified using different self-assembled monolayers (SAM) able to tune the electrostatic interaction between the protein and the substrate, depending on the nature of the terminal functional group in the SAM. The effects of protein immobilization time, electrode potential, solution pH and temperature, protein and O 2 concentration have been carefully investigated. Finally, direct electron transfer (DET) was investigated in the presence of the following inhibitors: fluoride (F −), chloride (Cl −) and azide (N − 3).
Oxygen Electroreduction versus Bioelectroreduction: Direct Electron Transfer Approach
Electroanalysis, 2016
Electroreduction and electrooxidation can be commonly referred to as electrocatalysis. Electroreduction processes occur in a variety of electrochemical devices, including sensors and electrolyzers, as well as fuel cells and some supercapacitors. These devices are used for analytical and synthetic purposes, as well as for energy conversion and storage, respectively. A variety of simple and more complex compounds can be used as oxidants, including hydronium ion (H 3 O +), organic and inorganic peroxides (ROOR'), nitric oxide (NO), nitrite (NO 2 À), and molecular oxygen (O 2). Among different reductive processes of different oxidants, reduction of O 2 is the key reaction not only in many natural and artificial systems, but also in many living organisms, i.e. aerobes. As the oxygen partial pressure in the atmosphere increased, aerobic organisms came to dominate the planet's species [1]. They, including humans, use the aerobic oxidation of different biofuels in order to extract as much energy as possible. Simultaneously, partial reduction of O 2 , occurring during aerobic respiration, will generate harmful reactive oxygen species, such as hydrogen peroxide (H 2 O 2), superoxide and hydroxyl radicals, which need to be safely disposed of by the organism. In many electrochemical devices similar problems exist, i.e. the complete direct four-electron O 2 reduction to the innocuous product H 2 O is not fully realized, and H 2 O 2 will be produced, which should be additionally utilized either by chemical decomposition or further two-electron electroreduction to H 2 O. This review paper is devoted to O 2 (bio)electroreduction, as it is the most common cathodic reaction in (bio)electrochemical systems.
Biotechnology Progress, 2011
The aim of this study was to examine the ability of an extracellular fungal laccase (LAC) to form colored products from simple non-colored organic precursors. Thirty different phenolic and non-phenolic precursors (o-, m-, and p-methoxy-, hydroxy-, sulfonic-, and aminosubstituted) were tested as single and coupled substrates in a LAC-catalyzed oxidation. The findings show that LAC catalyzes the formation of colored products (from yellow/brown to red and blue) by oxidation of single substrates that are benzene derivatives containing at least two substituents comprised of amino, hydroxy, and methoxy groups. All precursors were tested by cyclic voltammetry and the correlation between their structure and redox potential, and the possibility of their transformation into colored products by fungal LAC was found. Colored products were yielded from single substrates possessing a value of the oxidation peak (E o) lower than 1,150 mV vs. normal hydrogen electrode (NHE). Substrates with an oxidation peak higher than 1,150 mV vs. NHE were transformed by LAC into colored compounds only in the presence of an additional precursor characterized by a low value of E o and the presence of reactive substituents such as methoxy, hydroxy, and amino groups. Therefore, additional hydroxylation, methoxylation, and amination of phenolic and non-phenolic substrates may represent a strategy to increase the range of these compounds as potential dyes precursors. V
Advances in enzyme bioelectrochemistry
Anais da Academia Brasileira de Ciencias, 2018
Bioelectrochemistry can be defined as a branch of Chemical Science concerned with electron-proton transfer and transport involving biomolecules, as well as electrode reactions of redox enzymes. The bioelectrochemical reactions and system have direct impact in biotechnological development, in medical devices designing, in the behavior of DNA-protein complexes, in green-energy and bioenergy concepts, and make it possible an understanding of metabolism of all living organisms (e.g. humans) where biomolecules are integral to health and proper functioning. In the last years, many researchers have dedicated itself to study different redox enzymes by using electrochemistry, aiming to understand their mechanisms and to develop promising bioanodes and biocathodes for biofuel cells as well as to develop biosensors and implantable bioelectronics devices. Inside this scope, this review try to introduce and contemplate some relevant topics for enzyme bioelectrochemistry, such as the immobilizati...
Chemical Modifications of Laccase from White-Rot Basidiomycete Cerrena unicolor
Applied Biochemistry and Biotechnology, 2012
Laccases belong to the group of phenol oxidizes and constitute one of the most promising classes of enzymes for future use in various fields. For industrial and biotechnological purposes, laccases were among the first enzymes providing larger-scale applications such as removal of polyphenols or conversion of toxic compounds. The wood-degrading basidiomycete Cerrena unicolor C-139, reported in this study, is one of the high-laccase producers. In order to facilitate novel and more efficient biocatalytic process applications, there is a need for laccases with improved biochemical properties, such as thermostability or stability in broad ranges of pH. In this work, modifications of laccase isoforms by hydrophobization, hydrophilization, and polymerization were performed. The hydrophobized and hydrophilized enzyme showed enhanced surface activity and higher ranges of pH and temperatures in comparison to its native form. However, performed modifications did not appear to noticeably alter enzyme's native structure possibly due to the formation of coating by particles of saccharides around the molecule. Additionally, surface charge of modified laccase shifted towards the negative charge for the hydrophobized laccase forms. In all tested modifications, the size exclusion method led to average 80 % inhibition removal for hydrophilized samples after an hour of incubation with fluoride ions. Samples that were hydrophilized with lactose and cellobiose showed an additional 90 % reversibility of inhibition by fluoride ions after an hour of concluding the reaction and 40 % after 24 h. The hydrophobized laccase showed higher level of the reversibility after 1 h (above 80 %) and 24 h (above 70 %) incubation with fluoride ions. The addition of ascorbate to laccase solution before a fluoride spike resulted in more efficient reversibility of fluoride inhibitory effect in comparison to the treatments with reagents used in the reversed sequence.
Applied Sciences
The rapid growth of the human population in recent decades has resulted in the intensive development of various industries, the development of urban agglomerations and increased production of medicines for animals and humans, plant protection products and fertilizers on an unprecedented scale. Intensive agriculture, expanding urban areas and newly established industrial plants release huge amounts of pollutants into the environment, which, in nature, are very slowly degraded or not decomposed, which leads to their accumulation in water and terrestrial ecosystems. Researchers are scouring extremely contaminated environments to identify organisms that have the ability to degrade resistant xenobiotics, such as PAHs, some pharmaceuticals, plasticizers and dyes. These organisms are a potential source of enzymes that could be used in the bioremediation of industrial and municipal wastewater. Great hopes are pinned on oxidoreductases, including laccase, called by some a green biocatalyst b...
Collection of Czechoslovak Chemical Communications, 2016
What prompted you to investigate this topic/problem? Cellobiose dehydrogenase (CDH) is one of the few sugar oxidising enzymes that shows efficient direct electron transfer (DET) characteristics with electrodes and thus av ery good candidate for making third-generation biosensors and bioanodes for biofuel cells. However,DET relies on good communication between the cytochrome domain (CYT) and the electrode. On an aked electrode CDH is expected to adsorb randomly meaning that all CYTsw ill not make efficient contact with the electrode. In this study,w e combined two approaches to ensure advantageous orientation of as many CDH molecules as possible through:1)making the electrode surface positively charged using polyethyleneimine and 2) nanostructuring the electrode surface with gold nanoparticles. This combination increased both the percentage of better orientated CDH molecules and current density leading to the sensitive detection of lactose.
Sensors, 2018
Dehydrogenase based bioelectrocatalysis has been increasingly exploited in recent years in order to develop new bioelectrochemical devices, such as biosensors and biofuel cells, with improved performances. In some cases, dehydrogeases are able to directly exchange electrons with an appropriately designed electrode surface, without the need for an added redox mediator, allowing bioelectrocatalysis based on a direct electron transfer process. In this review we briefly describe the electron transfer mechanism of dehydrogenase enzymes and some of the characteristics required for bioelectrocatalysis reactions via a direct electron transfer mechanism. Special attention is given to cellobiose dehydrogenase and fructose dehydrogenase, which showed efficient direct electron transfer reactions. An overview of the most recent biosensors and biofuel cells based on the two dehydrogenases will be presented. The various strategies to prepare modified electrodes in order to improve the electron transfer properties of the device will be carefully investigated and all analytical parameters will be presented, discussed and compared.
BMC Biotechnology, 2019
Background: Laccases are multicopper oxidases, which are assigned into auxiliary activity family 1 (AA1) in the CAZy database. These enzymes, catalyzing the oxidation of phenolic and nonphenolic substrates coupled to reduction of O 2 to H 2 O, are increasingly attractive as eco-friendly oxidation biocatalysts. Basidiomycota laccases are well characterized due to their potential in de-lignification of lignocellulose. By contrast, insight into the biochemical diversity of Ascomycota counterparts from saprophytes and plant pathogens is scarce. Results: Here, we report the properties of the laccase from the major wheat pathogen Zymoseptoria tritici (ZtrLac1A), distinguished from common plant fungal pathogens by an apoplastic infection strategy. We demonstrate that ZtrLac1A is appended to a functional starch-binding module and displays an activity signature disfavoring relatively apolar phenolic redox mediators as compared to the related biochemically characterized laccases. By contrast, the redox potential of ZtrLac1A (370 mV vs. SHE) is similar to ascomycetes counterparts. The atypical specificity is consistent with distinctive sequence substitutions and insertions in loops flanking the T1 site and the enzyme C-terminus compared to characterized laccases. Conclusions: ZtrLac1A is the first reported modular laccase appended to a functional starch-specific carbohydrate binding module of family 20 (CBM20). The distinct specificity profile of ZtrLac1A correlates to structural differences in the active site region compared to previously described ascomycetes homologues. These differences are also highlighted by the clustering of the sequence of ZtrLac1A in a distinct clade populated predominantly by plant pathogens in the phylogenetic tree of AA1 laccases. The possible role of these laccases in vivo merits further investigations. These findings expand our toolbox of laccases for green oxidation and highlight the binding functionality of CBM-appended laccases as versatile immobilization tags.
New trends in the electrochemical sensing of dopamine
Analytical and Bioanalytical Chemistry, 2012
Since the early 70s electrochemistry has been used as a powerful analytical technique for monitoring electroactive species in living organisms. In particular, after extremely rapid evolution of new micro and nanotechnology it has been established as an invaluable technique ranging from experiments in vivo to measurement of exocytosis during communication between cells under in vitro conditions. This review highlights recent advances in the development of electrochemical sensors for selective sensing of one of the most important neurotransmitters-dopamine. Dopamine is an electroactive catecholamine neurotransmitter, abundant in the mammalian central nervous system, affecting both cognitive and behavioral functions of living organisms. We have not attempted to cover a large time-span nor to be comprehensive in presenting the vast literature devoted to electrochemical dopamine sensing. Instead, we have focused on the last five years, describing recent progress as well as showing some problems and directions for future development.