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• W2028164554 abstract "Abstract Three hemoproteins and five globular proteins containing SS-groups were investigated by several electrochemical methods in order to characterize the behaviour of proteins at the electrode and to elucidate the electron transfer in protein molecules. The surface area per adsorbed molecule determined by evaluation of adsorption kinetics and by means of radiochemical studies shows that the globular proteins investigated have an unfolded conformation at the electrode. The reduction of the hemoproteins is markedly influenced by strong adsorption effects. Nevertheless, the electron transfer is not limited to the molecules directly attached to the electrode surface and native reduction products were obtained by electrolysis. With hemoproteins an electron transfer through adsorbed molecules to freely diffusible particles is proposed. In contrast, the charge transfer through the protein fabric is inhibited at SS-reduction." @default.
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• W2028164554 date "1976-01-01" @default.
• W2028164554 modified "2023-09-27" @default.
• W2028164554 title "Interfacial behaviour and cathodic reduction of globular proteins" @default.
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• W2028164554 doi "https://doi.org/10.1016/0302-4598(76)80014-1" @default.
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