The electrochemical characteristics of blue copper protein monolayers on gold

Andolfi, Laura; Bruce, Delphine; Cannistraro, Salvatore; Canters, Gerard W.; Davis, Jason J.; Hill, H. Allen O.; Crozier, John; Verbeet, Martin Ph.; Wrathmell, C.L.; Astier, Yann

doi:10.1016/j.jelechem.2003.09.038

Cited by 73 publications

(81 citation statements)

References 41 publications

(53 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Electron transfer rate constants for plastocyanin and azurin at 20°C are listed in Table 1. As it is often the case with members of this protein family [12,20], electron exchange is about ten times faster for azurin than for plastocyanin.…”

Section: Fig 1 Illustrates Typical Voltammograms Of Adsorbed Plastocmentioning

confidence: 90%

Voltammetric study of the adsorbed thermophilic plastocyanin from Phormidium laminosum up to 90°C

Olloqui‐Sariego

Frutos-Beltrán

Roldán

et al. 2012

Electrochemistry Communications

View full text Add to dashboard Cite

Redox thermodynamics and kinetics of plastocyanin from Phormidium laminosum, and of azurin from Pseudonomas aeruginosa, have been investigated as a function of temperature by protein film voltammetry. To this purpose, both proteins have been physisorbed on a pyrolytic graphite edge electrode. A pronounced negative shift of the plastocyanin standard potential, compared to a slight shift in the case of azurin, has been found upon increasing the temperature. Hence, significant conformational and/or solvation changes accompany the redox conversion of plastocyanin. Lower electron transfer rate constants (by c.a. one order of magnitude) and higher activation enthalpies have been found for plastocyanin as compared to azurin. The voltammetric response of azurin vanishes irreversibly at temperatures close to 60°C, whereas the redox properties of plastocyanin remain unaltered, except for some loss of electroactive protein, after heating the electrode at temperatures as high as 90°C.

show abstract

Section: Fig 1 Illustrates Typical Voltammograms Of Adsorbed Plastocmentioning

confidence: 90%

Voltammetric study of the adsorbed thermophilic plastocyanin from Phormidium laminosum up to 90°C

Olloqui‐Sariego

Frutos-Beltrán

Roldán

et al. 2012

Electrochemistry Communications

View full text Add to dashboard Cite

show abstract

“…Due to their chemical inertness and unique optical properties (Jain et al 2008), the noble metals, gold and silver, are the most commonly used metals employed as probes or sensors in these techniques. Along with well-known applications of metal surfaces, such as biosensors and implants (Liu et al 2004), metal surfaces are also used in bioelectronics as electrodes as they allow controlled exchange of electrons with metalloproteins immobilized on them (Alessandrini et al 2005;Andolfi et al 2004). The interactions of proteins with bare metal surfaces have been the subject of many computational studies, which cover a wide range of different elemental and alloy surfaces, such as Cu(100) (Chen & Wang, 2010), Au(111) (Bizzarri, 2006;Hoefling et al 2011;Siwko & Corni, 2013;Venkat et al 2007;Zanetti-Polzi et al 2014), Au(100) (Hagiwara et al 2009), Au nanoparticle (Todorova et al 2014), Fe (Zhang et al 2009b), Ni (Yang & Zhao, 2006), Pd (Coppage et al 2011), Pt (Kantarci et al 2005, Ag (Aliaga et al 2011;Ghosh et al 2012) and steel (Imamura et al 2003).…”

Section: Elemental Metals and Alloysmentioning

confidence: 99%

Modeling and simulation of protein–surface interactions: achievements and challenges

Ozboyaci

Kokh

Corni

et al. 2016

Quart. Rev. Biophys.

184

199

View full text Add to dashboard Cite

Abstract. Understanding protein-inorganic surface interactions is central to the rational design of new tools in biomaterial sciences, nanobiotechnology and nanomedicine. Although a significant amount of experimental research on protein adsorption onto solid substrates has been reported, many aspects of the recognition and interaction mechanisms of biomolecules and inorganic surfaces are still unclear. Theoretical modeling and simulations provide complementary approaches for experimental studies, and they have been applied for exploring protein-surface binding mechanisms, the determinants of binding specificity towards different surfaces, as well as the thermodynamics and kinetics of adsorption. Although the general computational approaches employed to study the dynamics of proteins and materials are similar, the models and force-fields (FFs) used for describing the physical properties and interactions of material surfaces and biological molecules differ. In particular, FF and water models designed for use in biomolecular simulations are often not directly transferable to surface simulations and vice versa. The adsorption events span a wide range of time-and length-scales that vary from nanoseconds to days, and from nanometers to micrometers, respectively, rendering the use of multi-scale approaches unavoidable. Further, changes in the atomic structure of material surfaces that can lead to surface reconstruction, and in the structure of proteins that can result in complete denaturation of the adsorbed molecules, can create many intermediate structural and energetic states that complicate sampling. In this review, we address the challenges posed to theoretical and computational methods in achieving accurate descriptions of the physical, chemical and mechanical properties of protein-surface systems. In this context, we discuss the applicability of different modeling and simulation techniques ranging from quantum mechanics through all-atom molecular mechanics to coarse-grained approaches. We examine uses of different sampling methods, as well as free energy calculations. Furthermore, we review computational studies of protein-surface interactions and discuss the successes and limitations of current approaches.

show abstract

“…Azurin from Pseudomonas aeruginosa is commercially available, has a known protein sequence and crystal structure. Moreover, its spectral, electrochemical, and kinetic properties have been studied extensively (Brill et al, 1968;Soininen and Ellfolk, 1972;Van de Kamp et al, 1990;Nar et al, 1991;Solomon et al, 1992;Van Pouderoyen et al, 1997;Gray et al, 2000;Jeuken et al, 2002;Andolfi et al, 2004;Armstrong et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Electrochemical characterization and application of azurin-modified gold electrodes for detection of superoxide

Shleev

Wetterö

Magnusson

et al. 2006

Biosensors and Bioelectronics

View full text Add to dashboard Cite

The interaction of superoxide radicals with Pseudomonas aeruginosa azurin in solution and in adsorbed form was characterized using spectrophotometric and electrochemical techniques. It was determined that the rate constant for the reduction of azurin by superoxide ion in solution was about 10 5 M -1 s -1 , being 2-3 times lower than the constant for cytochrome c. To prepare superoxide sensitive electrode azurin was immobilised on the surface of gold electrodes. Cyclic voltammetry measurements revealed that the best electron transfer between the protein and the electrode is realised at short-chain thiol, viz. 3,3'-dithiobis(sulfosuccinimidylpropionate,)-(DTSSP-) modified gold. The formal potential of the redox protein on the DTSSP-modified electrode was found to be 380 mV vs. NHE being 100 mV more positive if compared to the standard redox potential of the T1 site of azurin fromPseudomonas aeruginosa. The heterogeneous electron transfer rate constant was determined to be in the range 2-6 s −1 for the azurin adsorbed on the DTSSP-modified gold electrodes.Based on the electrochemical measurements the sensitivity of the biosensor towards superoxide was calculated to be 6. biosensor displayed a response to chemically and enzymatically generated superoxide, and adequate sensitivity to assess the biological response of stimulated human neutrophils.

show abstract

The electrochemical characteristics of blue copper protein monolayers on gold

Cited by 73 publications

References 41 publications

Voltammetric study of the adsorbed thermophilic plastocyanin from Phormidium laminosum up to 90°C

Voltammetric study of the adsorbed thermophilic plastocyanin from Phormidium laminosum up to 90°C

Modeling and simulation of protein–surface interactions: achievements and challenges

Electrochemical characterization and application of azurin-modified gold electrodes for detection of superoxide

Contact Info

Product

Resources

About