Direct electrochemical reduction of ferredoxin promoted by Mg²⁺

Membrane-entrapped microperoxidase as a ‘solid-state’ promoter in the electrochemistry of soluble metalloproteins

“…From the cyclic voltammograms shown in Fig. 3(c) we find that the AEP value increases with the scan rate, as already observed for other proteins [16,17] (the lowest value of 80 mV being obtained at a scan rate of 5 mV/s). The calculated value for the redox potential E1 = + 0.300 V versus the standard hydrogen electrode is not inconsistent with the potentiometric value reported in the literature [18] under similar experimental conditions (+0.330 V versus the standard hydrogen electrode at neutral pH).…”

Electrochemical behaviour of low-potential electron-transferring proteins at the mercury electrode

“…Since no data are available on the formal potentials of M. elsdenii ferredoxin and rubredoxin it is assumed that, in analogy with spinach ferredoxin, the formal potentials are those obtained at optimal reduction efficiency; -612 mV and -250 mV respectively. Recently Armstrong et al [55] have determined the formal potential of Clostridium pasteurianum ferredoxin by means of cyclovoltammetry. They found a value of -614 mV, which is identical to the value we determined for M. elsdenii ferredoxin.…”

A precursor-approach in constructing 3D ITO electrodes for the improved performance of photosystem I-cyt c photobioelectrodes

“…[70][71][72][73][74] Moreover, the reorganization energy of the participating molecules is crucial and reflects structural rigidity of the two species and thus, the eagerness to exchange electrons: the lower the reorganization energy of participants in an electrochemical event is, the higher is k ET . Until now, many other redox-active proteins and enzymes have been demonstrated to exchange electrons directly at modified electrodes: a) Cu-redox proteins: azurin, 75,76 hemocyanin, 76,77 plastocyanin, 78 b) Fe-redox proteins: cytochrome c, [79][80][81][82][83][84][85] ferredoxin, 86,87…”