2012
DOI: 10.1016/j.jelechem.2011.12.012
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Activation of laccase bioelectrocatalysis of O2 reduction to H2O by carbon nanoparticles

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Cited by 35 publications
(29 citation statements)
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“…Thus, we expected different surface compatibility between the overall negatively charged CDH, positively charged cyt c and differently charged CNPs, though the productive ET could be expected also for similarly charged surfaces and proteins as was previously demonstrated. [22] Along with that, in lower ionic strength solutions ( Figure S1) and in pure water [9] unmodified CNP possess significant negative charge, due to graphitic edge planes on the CNP surface with phenolic, quinoid and carboxylic surface functionalities. [21]…”
Section: Resultsmentioning
confidence: 74%
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“…Thus, we expected different surface compatibility between the overall negatively charged CDH, positively charged cyt c and differently charged CNPs, though the productive ET could be expected also for similarly charged surfaces and proteins as was previously demonstrated. [22] Along with that, in lower ionic strength solutions ( Figure S1) and in pure water [9] unmodified CNP possess significant negative charge, due to graphitic edge planes on the CNP surface with phenolic, quinoid and carboxylic surface functionalities. [21]…”
Section: Resultsmentioning
confidence: 74%
“…From this perspective, the most plausible explanation for the bioelectrocatalysis activation seems to be CDH-CNPs interactions introducing interfacial/conformational changes in the CDH's heme domain that enhance the CDH-ferricyanide reactivity (Figure 6a,b). The probability of the previously discussed allosteric regulation of bioelectrocatalysis by CNPs [9] is low. Considering different surface properties of CNPs used (their different charge), CNP and CNP-very likely interact with different surface domains of Humicola insolens CDH (overall, negatively charged) that are compatible with surface properties of the specific CNPs.…”
Section: Discussion Of the Mechanisms Of Cnps Actionmentioning
confidence: 92%
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“…In the absence of immobilized ABTS mediator from A‐felt, the current density is only approximately 30 % lower, which indicates that the adsorbed enzyme is well oriented for direct electron transfer (DET) between the electrode, the copper centers of laccase, and the oxygen molecules. DET with laccase enzyme has already been reported 2830. However, in this case, the open‐circuit voltage (OCV) is 0.34 V, as fixed by the polypyrrole electroconductivity, which also participates in electron transfer.…”
Section: Resultsmentioning
confidence: 93%
“…DET with laccase enzyme has already been reported. [28][29][30] However, in this case, the open-circuit voltage (OCV) is 0.34 V, as fixed by the polypyrrole electroconductivity, which also participates in electron transfer. If laccase and ABTS are co-immobilized on A-felt electrodes, the bio-electroreduction of oxygen is enhanced; this results not only in higher cathodic currents, but also in a modulation of the OCV values at which oxygen reduction begins: approximately 0.34 V in the absence of ABTS and approximately 0.53 V for the laccase + ABTS couple.…”
Section: Preparation and Characterization Of Bioelectrodesmentioning
confidence: 97%