Vitamin B12–transport protein interaction: electrochemistry of aquo- and glutathionyl-cobalamins adsorbed on carbon electrodes; role of the nucleotide chain
Identifieur interne : 000D78 ( Main/Exploration ); précédent : 000D77; suivant : 000D79Vitamin B12–transport protein interaction: electrochemistry of aquo- and glutathionyl-cobalamins adsorbed on carbon electrodes; role of the nucleotide chain
Auteurs : Lydie Ngandu [France] ; Dominique Robin [France] ; Asma El Kasmi [Maroc] ; Doris Lexa [France]Source :
- Inorganica Chimica Acta [ 0020-1693 ] ; 1999.
Descripteurs français
- Wicri :
- topic : électrochimie.
English descriptors
- KwdEn :
- B12a, Co(III)balamin, B12r, Co(II)balamin, B12s, Co(I)balamin, BR, Britton–Robinson, Bzm, benzimidazole, CV, cyclic voltammetry, Cbi, cobinamide, Cbl, cobalamin, Cobalamins, EPG, edge plane pyrolytic graphite, Electrochemistry, GC, glassy carbon, GSH, reduced glutathione, IF, intrinsic factor, NIF, non-intrinsic factor, SCE, saturated calomel electrode, Vitamin B12 derivatives.
Abstract
Several vitamin B12 derivatives (aquo, acetato, and glutathionyl cobalamins) adsorbed on an edge pyrolytic graphite electrode are studied in order to determine how their electrochemical behaviors are influenced by either the direct adsorption on the electrode material, or the adsorption in the presence of transport proteins, intrinsic factor (IF) and non-intrinsic factor (NIF). Comparison with the interfacial electrochemistry of the cobinamide demonstrates that, at neutral pH, the benzimidazole (Bzm) moiety is still coordinated to the Co(III) and Co(II) oxidized states of the adsorbed cobalamins. On the other hand, adsorption on pyrolytic graphite electrodes is shown to accelerate the kinetics for the reduction Co(III)/Co(II) when strong coordination by glutathione is involved compared to the results obtained in solution. The transport protein–cobalamin complexes are still reducible on the electrode. The potentials are not really changed for the IF complex while Co(II) is slightly more difficult to reduce in the case of the NIF complex.
Url:
DOI: 10.1016/S0020-1693(99)00193-0
Affiliations:
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Le document en format XML
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<term>BR, Britton–Robinson</term>
<term>Bzm, benzimidazole</term>
<term>CV, cyclic voltammetry</term>
<term>Cbi, cobinamide</term>
<term>Cbl, cobalamin</term>
<term>Cobalamins</term>
<term>EPG, edge plane pyrolytic graphite</term>
<term>Electrochemistry</term>
<term>GC, glassy carbon</term>
<term>GSH, reduced glutathione</term>
<term>IF, intrinsic factor</term>
<term>NIF, non-intrinsic factor</term>
<term>SCE, saturated calomel electrode</term>
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<front><div type="abstract" xml:lang="en">Several vitamin B12 derivatives (aquo, acetato, and glutathionyl cobalamins) adsorbed on an edge pyrolytic graphite electrode are studied in order to determine how their electrochemical behaviors are influenced by either the direct adsorption on the electrode material, or the adsorption in the presence of transport proteins, intrinsic factor (IF) and non-intrinsic factor (NIF). Comparison with the interfacial electrochemistry of the cobinamide demonstrates that, at neutral pH, the benzimidazole (Bzm) moiety is still coordinated to the Co(III) and Co(II) oxidized states of the adsorbed cobalamins. On the other hand, adsorption on pyrolytic graphite electrodes is shown to accelerate the kinetics for the reduction Co(III)/Co(II) when strong coordination by glutathione is involved compared to the results obtained in solution. The transport protein–cobalamin complexes are still reducible on the electrode. The potentials are not really changed for the IF complex while Co(II) is slightly more difficult to reduce in the case of the NIF complex.</div>
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