2004
DOI: 10.1016/j.jelechem.2003.09.038
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The electrochemical characteristics of blue copper protein monolayers on gold

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Cited by 73 publications
(82 citation statements)
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References 41 publications
(53 reference statements)
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“…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%
“…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%
“…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%
“…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%